R&D Systems代理DPG00 Human PlGF Quantikine ELISA Kit (1 KT)

2025-06-28

货号:DPG00

品牌:R&D Systems

规格:1KT

目录价:¥7420.00

市场价格:¥5936.00

会员价格:¥5936.00

  • 到货时间:3~4周

    金山科研平台,产品价格货期咨询微信:jinshanbio Assay Type:Solid Phase Sandwich ELISA Format:96-well strip plate Assay Length:3.5 hours or 4.5 hours Sample Type & Volume Required Per Well:Cell Culture Supernates (100 µL), Serum (100 µL), EDTA Plasma (100 µL), Heparin Plasma (100 µL), Citrate Plasma (100 µL), Urine (100 µL) Sensitivity:7 pg/mL Assay Range:15.6 - 1,000 pg/mL (Serum, Heparin Plasma, Cell Culture Supernates, Citrate Plasma, EDTA Plasma, Urine) Specificity:Natural and recombinant human PlGF Cross-reactivity:Cross-reactivity observed with 1 or more available related molecules. Cross-species reactivity not tested. Interference:Interference observed with 1 or more available related molecules. Molecule Information: PlGF Long Name: Placenta Growth Factor Aliases: PGF; PGFL Entrez Gene IDs: 5228 (Human); 18654 (Mouse) Background: PlGF

    View PlGF IHC images. 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 PlGF that is the equivalent of human PlGF-2 has been identified. Human PlGF-1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF, respectively. 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/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 PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF-2, but not PlGF-1, shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2. 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.

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