Eumorphia

Multi-factors have been reported to have an effect on the intestine microbiome, together with genotype, age, eating regimen, and diet. Nevertheless, few experiences have investigated the relative capability of various elements to form the intestine microbiome in a single research.

Our design used a genetic Vitamin A poor mouse mannequin, the Rbp4^-/- mouse, feeding with the low Vitamin A diets at totally different ages of initiation (four or 7 weeks) for 28 days. Fecal samples had been collected for bacterial profiling at seven time factors after eating regimen controlling.

With RBP4 depletion, Akkermansia decreased and Bacteroides elevated, whereas Desulfovibrio, Barnesiella, Clostridium_XlVa, and Lactobacillus fluctuated. The bacterial group swiftly adjusted with the Vitamin A-deficient eating regimen administration and step by step modified (e.g., lower of Barnesiella and improve of Desulfovibrio).

Age exerted a comparatively weaker however long-last affect. At an earlier age to feed a Vitamin-A poor eating regimen, a better microbial dysbiosis index (MDI) will probably be valued. Of notice, the shaping results of eating regimen and age on the bacterial group various with the distinction of genotype, which could point out a better function of genotype than eating regimen and age in shaping the intestine microbiome.

Sarcopenia results in lack of skeletal muscle mass, high quality, and energy as a consequence of growing old; it was lately given a illness code (Worldwide Classification of Illnesses, Tenth Revision, Medical Modification, M62.84). Consequently, lately, sarcopenia-related analysis has elevated.

As well as, numerous research in search of to forestall and deal with sarcopenia by figuring out the varied mechanisms associated to the discount of skeletal muscle properties have been carried out. Earlier research have recognized muscle synthesis and breakdown; investigating them has generated proof for stopping and treating sarcopenia.

Mouse fashions are nonetheless essentially the most helpful ones for figuring out mechanisms underlying sarcopenia by correlations and interventions involving particular genes and their phenotypes. Mouse fashions used to check sarcopenia typically induce muscle atrophy by hindlimb unloading, denervation, or immobilization.

Although it’s much less regularly used, the senescence-accelerated mouse may also be helpful for sarcopenia analysis. Herein, we focus on instances the place senescence-accelerated and genetically engineered mouse fashions had been utilized in sarcopenia analysis and totally different views to make use of them.

Hemophilia A (HA), a standard bleeding dysfunction attributable to a deficiency of coagulation issue VIII (FVIII), has lengthy been thought-about a beautiful goal for gene remedy research. Nevertheless, full-length F8 cDNA can’t be packaged effectively by adeno-associated virus (AAV) vectors.

Because the second most prevalent mutation inflicting extreme HA, F8 intron 1 inversion (Inv1) is attributable to an intrachromosomal recombination, leaving the vast majority of F8 (exons 2-26) untranscribed. In concept, the truncated gene could possibly be rescued by integrating a promoter and the coding sequence of exon 1. To check this technique in vivo, we generated an HA mouse mannequin by deleting the promoter area and exon 1 of F8.

Donor DNA and CRISPR/SaCas9 had been packaged into AAV vectors and injected into HA mice intravenously. After remedy, F8 expression was restored and activated partial thromboplastin time (aPTT) was shortened. We additionally in contrast two liver-specific promoters and two forms of integrating donor vectors.

When an lively promoter was used, all the handled mice survived the tail-clip problem. That is the primary report of an in vivo gene restore technique with the potential to deal with a recurrent mutation in HA sufferers.

Epidemiological research have proven that carrot consumption could also be related to a decrease threat of growing a number of metabolic dysfunctions. Our group beforehand decided that the Bolero (Bo) carrot selection exhibited vascular and hepatic tropism utilizing mobile fashions of cardiometabolic ailments.

The current research evaluated the potential metabolic and cardiovascular protecting impact of Bo, grown underneath two circumstances (commonplace and biotic stress circumstances (BoBS)), in apolipoprotein E-knockout (ApoE^-/-) mice fed with excessive fats eating regimen (HFD).

Results on metabolic/hemodynamic parameters and on atherosclerotic lesions have been assessed. Each Bo and BoBS decreased plasma triglyceride and expression ranges of genes implicated in hepatic de novo lipogenesis and lipid oxidation. BoBS supplementation decreased physique weight achieve, secretion of very-low-density lipoprotein, and elevated cecal propionate content material.

Curiously, Bo and BoBS supplementation improved hemodynamic parameters by lowering systolic, diastolic, and imply blood strain. Furthermore, Bo improved cardiac output. Lastly, Bo and BoBS considerably diminished the aortic root lesion space.

These outcomes confirmed that Bo and BoBS enriched diets corrected a lot of the metabolic and cardiovascular issues in an atherosclerosis-prone genetic mouse mannequin and will subsequently signify an fascinating dietary method for the prevention of cardiovascular ailments.

Regardless of current advances on the whole most cancers remedy, glioblastoma stays among the many most deadly of human malignancies. Even with aggressive multimodal radiation and chemotherapy after surgical procedure, glioblastoma recurs with a bleak prognosis.

Many years of analysis centered on methods corresponding to rising radiation sensitivity and interference with oncogenic sign transduction have yielded solely incremental enhancements at finest. That is due partially to the radioresistance of glioblastoma and molecular heterogeneity of tumor cells.

We hypothesize is that the event of simpler glioblastoma therapies would require: (i) a extra correct molecular evaluation of glioblastoma in order to foretell response to remedy; (ii) higher genetically engineered mouse fashions, which may faithfully recapitulate human glioblastoma and the tumor microenvironment to check new approaches and (iii) growth and utility of extra correct and centered strategies to ship sustained excessive vitality particles to glioblastoma tumor websites.

This chapter describes the present state-of-the-art molecular evaluation approaches, newest in glioma mouse modelling, and advances within the utility of proton remedy remedy and analysis. By integrating primary and scientific analysis with cutting-edge applied sciences, a mechanistic understanding of glioblastoma remedy resistance and pathogenesis and the event of recent therapeutics to beat the therapeutic resistance of glioblastoma will probably be superior.

Abnormalities in electroencephalographic (EEG) biomarkers happen in sufferers with schizophrenia and people clinically at excessive threat for transition to psychosis and are related to cognitive impairment. Converging proof suggests N-methyl-D-aspartate receptor (NMDAR) hypofunction performs a central function within the pathophysiology of schizophrenia and sure contributes to biomarker impairments.

Thus, characterizing these biomarkers is of great curiosity for early analysis of schizophrenia and growth of novel remedies. We utilized in vivo EEG recordings and behavioral analyses to carry out a battery of electrophysiological biomarkers in a longtime mannequin of persistent NMDAR hypofunction, serine racemase knockout (SRKO) mice, and their wild-type littermates.

SRKO mice displayed impairments in investigation-elicited gamma energy that corresponded with diminished short-term social recognition and enhanced background (pre-investigation) gamma exercise. Moreover, SRKO mice exhibited sensory gating impairments in each evoked-gamma energy and event-related potential amplitude.

Nevertheless, different biomarkers together with the auditory steady-state response, sleep spindles, and state-specific energy spectral density had been typically neurotypical. In conclusion, SRKO mice display how persistent NMDAR hypofunction contributes to deficits in sure translationally-relevant EEG biomarkers altered in schizophrenia.

Mouse Anti-Human PlGF-2
MBS692571-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human PlGF-2
MBS692571-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Monoclonal anti-human PlGF
hAP-0010	Angio Proteomie	100ug	EUR 250

Mouse PlGF
MBS691520-0002mg	MyBiosource	0.002mg	EUR 265

Mouse PlGF
MBS691520-5x0002mg	MyBiosource	5x0.002mg	EUR 890

Mouse PlGF
MBS692108-0005mg	MyBiosource	0.005mg	EUR 350

Mouse PlGF
MBS692108-5x0005mg	MyBiosource	5x0.005mg	EUR 1275

Mouse PlGF
MBS692180-002mg	MyBiosource	0.02mg	EUR 625

Mouse PlGF
MBS692180-5x002mg	MyBiosource	5x0.02mg	EUR 2510

Mouse Monoclonal anti-Human PlGF Antibody
xAP-0457	Angio Proteomie	100ug	EUR 280

Anti-Mouse PlGF Antibody
103-M03	ReliaTech	100 µg	EUR 399
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively. Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF-2 has been identified. Mouse PlGF shares 60%, 92%, 62% and 59% aa identity with the appropriate isoform of human, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during human pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt-1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis. However, PlGF (especially human PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF-2, like VEGF164/165, shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2 and can inhibit nerve growth cone collapse. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic P lGF antibodies are being investigated to inhibit tumor growth and angiogenesis.

Anti-Mouse PlGF Antibody
103-PA04AG	ReliaTech	50 µg	EUR 157.5
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

Anti-Mouse PlGF Antibody
103-PA04S	ReliaTech	100 µg	EUR 126
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

Anti-Mouse PlGF Antibody
MBS4158465-01mg	MyBiosource	0.1mg	EUR 1255

Anti-Mouse PlGF Antibody
MBS4158465-5x01mg	MyBiosource	5x0.1mg	EUR 5390

Rabbit Anti-Mouse PlGF
103-PA04	Angio Proteomie	100ug	EUR 240

Anti-Human PGF/PlGF/PLGF Nanobody
MBS1568114-01mg	MyBiosource	0.1mg	EUR 405

Anti-Human PGF/PlGF/PLGF Nanobody
MBS1568114-5x01mg	MyBiosource	5x0.1mg	EUR 1520

Mouse PLGF ELISA Kit
EMP0025	Abclonal	96Tests	EUR 625.2

Mouse PlGF Rabbit pAb
A24547	Abclonal	20μL	EUR 262.15

PLGF (PGF) (PlGF-1/2) mouse monoclonal antibody, clone 178/G10, Purified
DM3525	Origene Technologies GmbH	100 µg	Ask for price

Mouse PlGF-2 ELISA Kit
E16ME0045	EnoGene	96T	EUR 833.33

Mouse PlGF-2 ELISA Kit
MBS8291429-5x96Tests	MyBiosource	5x96Tests	EUR 2755

Mouse PlGF-2 ELISA Kit
MBS8291429-96Tests	MyBiosource	96Tests	EUR 620

Mouse PlGF Recombinant Protein
M30-019	ReliaTech	5 µg	EUR 136.5
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

Mouse PlGF Recombinant Protein
M30-019S	ReliaTech	2 µg	EUR 73.5
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF-1, PlGF-2 and PlGF-3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF-2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF-2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

Mouse PlGF Recombinant Protein
M30-020	ReliaTech	20 µg	EUR 313.95
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

PLGF (Mouse, monoclonal, antagonistic)
mP1002r-m	Angio Proteomie	100ug	EUR 467.5

PLGF (PGF) (PlGF-1/2) mouse monoclonal antibody, clone 178/G10, Biotin, Purified
DM3525B	Origene Technologies GmbH	50 µg	Ask for price

Rat Monoclonal anti-mouse PlGF
mAP-0010	Angio Proteomie	100ug	EUR 250

Mouse PLGF-2 PicoKine ELISA Kit
EK0863	BosterBio	96 wells	EUR 510
Description: For Quantitative Detection of mouse PLGF-2 in cell culture supernates, serum and plasma (heparin, EDTA).

Mouse PLGF-2 PicoKine ELISA Kit
MBS1751078-5x96StripWells	MyBiosource	5x96-Strip-Wells	EUR 2755

Mouse PLGF-2 PicoKine ELISA Kit
MBS1751078-96StripWells	MyBiosource	96-Strip-Wells	EUR 600

PLGF (PGF) mouse monoclonal antibody, clone PLGF94, Purified
AM50307PU-S	Origene Technologies GmbH	100 µg	Ask for price

PLGF (PGF) mouse monoclonal antibody, clone PLGF94, Purified
AM50307PU-T	Origene Technologies GmbH	20 µg	Ask for price

Recombinant Mouse PLGF/PGF Protein
MBS9144052-002mg	MyBiosource	0.02mg	EUR 235

Recombinant Mouse PLGF/PGF Protein
MBS9144052-005mg	MyBiosource	0.05mg	EUR 320

Recombinant Mouse PLGF/PGF Protein
MBS9144052-01mg	MyBiosource	0.1mg	EUR 460

Recombinant Mouse PLGF/PGF Protein
MBS9144052-5x01mg	MyBiosource	5x0.1mg	EUR 1900

Purified recombinant Mouse PLGF protein
MBS5308876-001mg	MyBiosource	0.01mg	EUR 380

Purified recombinant Mouse PLGF protein
MBS5308876-5x001mg	MyBiosource	5x0.01mg	EUR 1660

Mouse PLGF / PGF Protein, His Tag
PGF-M52H0	ACROBIOSYSTEMS	50ug	EUR 3327.7
Description: Mouse PLGF, His Tag (PGF-M52H0) is expressed from human 293 cells (HEK293). It contains AA Val 19 - Pro 158 (Accession # P49764-1).

Anti-Rat PlGF Antibody
104-PA04AG	ReliaTech	50 µg	EUR 157.5
Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.

Anti-Rat PlGF Antibody
104-PA04S	ReliaTech	100 µg	EUR 126
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively. Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus. In rat only one PlGF that is the equivalent of human PlGF-2 has been identified. Rat PlGF shares 60%, 92%, 62% and 59% aa identity with the appropriate isoform of human, mouse, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during human pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt-1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis. However, PlGF (especially human PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF-2, like VEGF164/165, shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2 and can inhibit nerve growth cone collapse. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic PlGF antibodies are being investigated to inhibit tumor growth and angiogenesis.

Rabbit anti PlGF (human)
102-PA04AG	Angio Proteomie	50ug	EUR 240

Rabbit anti PlGF (human)
102-PA04S	Angio Proteomie	100ug	EUR 240

Rabbit Anti-Rat PlGF
104-PA04	Angio Proteomie	100ug	EUR 240

RABBIT ANTI HUMAN PLGF
MBS222860-01mg	MyBiosource	0.1mg	EUR 660

RABBIT ANTI HUMAN PLGF
MBS222860-5x01mg	MyBiosource	5x0.1mg	EUR 2795

Anti-Human PlGF Antibody
101-M03	ReliaTech	100 µg	EUR 378
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF Antibody
101-M67	ReliaTech	100 µg	EUR 189
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF Antibody
101-M69	ReliaTech	100 µg	EUR 189
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF Antibody
101-MBi67	ReliaTech	50 µg	EUR 189
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF Antibody
102-P248	ReliaTech	100 µg	EUR 245.7
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF Antibody
MBS4158489-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human PlGF Antibody
MBS4158489-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human PlGF-2 Antibody
101-M65	ReliaTech	100 µg	EUR 246.75
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-Human PlGF-2 Antibody
101-M65A	ReliaTech	100 µg	EUR 246.75
Description: Placenta Growth Factor-2 (PlGF-2), a 22 kDa protein consisting of 152 amino acid residues is produced as a homodimer. PlGF is a polypeptide growth factor and a member of the platelet-derived growth factor family but more related to vascular endothelial growth factor (VEGF). PlGF acts only as a weak mitogen for those cell types possessing receptors for binding (e.g. vascular endothelial cells). At least one high-affinity receptor for PlGF (FLT-1 or VEGF-R1) has been demonstrated in different primary cell types (e.g. human umbilical vein endothelial cells and monocytes). In addition to its action as a weak mitogen it is also a chemoattractant for monocytes and endothelial cells. Three different proteins are generated by differential splicing of the human PlGF gene: PlGF-1 (131aa native chain), PlGF-2 (152aa) and PlGF-3 (203aa). All 3 mitogens are secretable proteins, but PlGF-2 can bind to heparin with high affinity. PlGF is apparently a homodimer, but preparations of PlGF show some heterogeneity on SDS gels depending of the varying degrees of glycosylation. All dimeric forms possess similar biological activities. Heterodimers between VEGF and PlGF are mitogenic for endothelial cells and have strong angiogenic activity in vivo (e.g. in the CAM assay or in the cornea pocket assay). Different cells and tissues (e.g. placenta) express PlGF-1 and PlGF-2 at different rates. A much related protein of PlGF is VEGF with about 53% homology and VEGF-B with similar biological activities.

OKRC01283-96W - PLGF-2 ELISA Kit (Mouse)
OKRC01283-96W	Aviva Systems Biology	96Wells	EUR 525

Mouse PLGF/PGF HEK293 Overexpression Lysate
MBS8116397-03mg	MyBiosource	0.3mg	EUR 280

Mouse PLGF/PGF HEK293 Overexpression Lysate
MBS8116397-5x03mg	MyBiosource	5x0.3mg	EUR 1205

Mouse PLGF/PGF HEK293 Overexpression Lysate
MBS8116398-03mg	MyBiosource	0.3mg	EUR 280

Mouse PLGF/PGF HEK293 Overexpression Lysate
MBS8116398-5x03mg	MyBiosource	5x0.3mg	EUR 1205

Placenta Growth Factor (PLGF) Polyclonal Antibody (Mouse)
4-PAA114Mu01	Cloud-Clone	Ask for price Ask for price Ask for price Ask for price Ask for price	100ul 10ml 1ml 200ul 20ul
Description: A Rabbit polyclonal antibody against Mouse Placenta Growth Factor (PLGF)

Mouse Placenta Growth Factor (PLGF) Protein
20-abx068553	Abbexa	Ask for price Ask for price Ask for price Ask for price Ask for price	100 ug 10 ug 1 mg 200 ug 50 ug

Mouse Placenta Growth Factor (PLGF) Protein
abx068553-20g	Abbexa	20 µg	EUR 562.5

Mouse Placenta Growth Factor (PLGF) Protein
abx068553-5g	Abbexa	5 µg	EUR 287.5

PLGF(PLGF93) Antibody
BNC810093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF680R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC810093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF680R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC810094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF680R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC810094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF680R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC430093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF543 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC430093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF543 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC430094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF543 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC430094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF543 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC050093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF405M conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC050093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF405M conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC050094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF405M conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC050094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF405M conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC550093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF555 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC550093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF555 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC550094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF555 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC550094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF555 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC610093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF660R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC610093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF660R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC610094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF660R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC610094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF660R conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC800093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF680 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC800093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF680 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC800094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF680 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC800094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF680 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC700093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), CF770 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNC700093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), CF770 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC700094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), CF770 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNC700094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), CF770 conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCP0093-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF93), PerCP conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCP0094-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF94), PerCP conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCR0093-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF93), RPE conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCR0094-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF94), RPE conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCA0093-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF93), APC conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCA0094-250	Biotium	250uL	EUR 459.6
Description: Primary antibody against PLGF(PLGF94), APC conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCAP0093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCAP0093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCAP0094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCAP0094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCH0093-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF93), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF93) Antibody
BNCH0093-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF93), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCH0094-100	Biotium	100uL	EUR 238.8
Description: Primary antibody against PLGF(PLGF94), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

PLGF(PLGF94) Antibody
BNCH0094-500	Biotium	500uL	EUR 652.8
Description: Primary antibody against PLGF(PLGF94), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL

Mouse PLGF(Placenta Growth Factor) ELISA Kit
ELK1242-48T	ELK Biotech	48T	Ask for price
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PLGF. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PLGF. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PLGF, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PLGF in the samples is then determined by comparing the OD of the samples to the standard curve.

Mouse PLGF(Placenta Growth Factor) ELISA Kit
ELK1242-96T	ELK Biotech	96T	Ask for price
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PLGF. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PLGF. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PLGF, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PLGF in the samples is then determined by comparing the OD of the samples to the standard curve.

Mouse PLGF (Placenta Growth Factor) ELISA Kit
MBS8800244-10x96StripWells	MyBiosource	10x96-Strip-Wells	EUR 3130

Mouse PLGF (Placenta Growth Factor) ELISA Kit
MBS8800244-48StripWells	MyBiosource	48-Strip-Wells	EUR 315

Mouse PLGF (Placenta Growth Factor) ELISA Kit
MBS8800244-5x96StripWells	MyBiosource	5x96-Strip-Wells	EUR 1710

Mouse PLGF (Placenta Growth Factor) ELISA Kit
MBS8800244-96StripWells	MyBiosource	96-Strip-Wells	EUR 385

Anti-Human PGF/PlGF Antibody
MBS1569264-01mg	MyBiosource	0.1mg	EUR 375

Anti-Human PGF/PlGF Antibody
MBS1569264-5x01mg	MyBiosource	5x0.1mg	EUR 1390

Anti-Human PlGF (native) Antibody
102-PABi04	ReliaTech	50 µg	EUR 157.5
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Anti-PGF/Plgf Picoband Antibody
MBS1750586-01mg	MyBiosource	0.1mg	EUR 450

Anti-PGF/Plgf Picoband Antibody
MBS1750586-5x01mg	MyBiosource	5x0.1mg	EUR 1870

Anti-Human PlGF (Peptide) Antibody
102-PA01S	ReliaTech	100 µg	EUR 115.5
Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.

Rabbit Anti-Human PlGF (native)
102-PA04	Angio Proteomie	100ug	EUR 240

Polyclonal Anti-PGF (PLGF) Antibody
GWB-BBP088	GenWay Biotech	0.1 mg	Ask for price

Rabbit Anti-Human PlGF (Peptide)
102-PA01	Angio Proteomie	100ug	EUR 240

PLGF/PGF Protein, Mouse, Recombinant (hFc Tag)
MBS8122547-005mg	MyBiosource	0.05mg	EUR 340

PLGF/PGF Protein, Mouse, Recombinant (hFc Tag)
MBS8122547-05mg	MyBiosource	0.5mg	EUR 1825

PLGF/PGF Protein, Mouse, Recombinant (hFc Tag)
MBS8122547-5x05mg	MyBiosource	5x0.5mg	EUR 8060

Placenta Growth Factor (PLGF) Polyclonal Antibody (Mouse), PE
4-PAA114Mu01-PE	Cloud-Clone	Ask for price Ask for price Ask for price Ask for price Ask for price	100ul 10ml 1ml 200ul 20ul
Description: A Rabbit polyclonal antibody against Mouse Placenta Growth Factor (PLGF). This antibody is labeled with PE.

Mouse Placenta Growth Factor (PLGF) ELISA Kit
DLR-PLGF-Mu	DL Develop	96T	EUR 241
Description: serum, plasma, tissue homogenates or other biological fluids.

Mouse Placenta Growth Factor (PLGF) ELISA Kit
DLR-PLGF-Mu-48T	DL Develop	48T	EUR 380.4
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Placenta Growth Factor (PLGF) in samples from serum, plasma, tissue homogenates or other biological fluids.

Importantly, our gamma band findings counsel an aberrant signal-to-noise ratio impairing cognition that happens with NMDAR hypofunction, doubtlessly tied to impaired task-dependent alteration in useful connectivity.