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Distributed product

Q-Plex™ Human PDGF

  • Regulatory status:RUO
  • Type:Singleplex Assays
  • Other names:PDGF
  • Species:Human
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Cat. No. Size Price


468649HU 96 wells (1 kit)
PubMed Product Details
Technical Data

Cat # changed from RQS468649HU to 468649HU

Type

Singleplex Assays

Applications

Serum, Plasma

Sample Requirements

50 µl/well

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date.

Calibration Range

4000–5.49 pg/mL

Summary

Features

  • For research use only
  • Detection Method: Chemiluminescent
  • The kit measures Human PDGF
  • This kit is validated for use with plasma, serum
  • Wide range across the standard curve means fewer dilutions per sample.
  • Better sensitivity than traditional ELISAs capture low analyte levels.
  • High end range captures data for concentrated samples.
  • Intra-well precision from replicate micro-spots provides greater assurity of results
  • Easy to use ELISA protocol

Summary

Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGFAA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domaincontaining molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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