Anti-PDGFR Beta Antibody

Evaluated by Western Blotting in BALB/3T3 clone A31 cell lysate.

Western Blotting Analysis: 2 µg/mL of this antibody detected PDGFR in 10 µg of BALB/3T3 clone A31 cell lysate.

Detect Platelet-derived growth factor receptor beta using this rabbit polyclonal Anti-PDGFR Beta Antibody, Cat. No. 06-498-I, validated for use in Immunocytochemistry, Immunoprecipitation, and Western Blotting.

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected PDGFR immunoreactivity in 4% paraformaldehyde-fixed, 0.3% Triton X-100-permeabilized BALB/3T3 clone A31 cells.

Immunoprecipitation Analysis: 5 µg from a representative lot immunoprecipitated PDGFR from 500 µg of BALB/3T3 clone A31 cell lysate.

Research Category
Signaling

This polyclonal antibody targets a cytoplasmic sequence C-terminal to the PDGFR kinase domain.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Platelet-derived growth factor receptor beta (EC 2.7.10.1; UniProt P09619; also known as Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, CD140b, PDGF-R-beta, PDGFR-1, PDGFR-beta, Platelet-derived growth factor receptor 1) is encoded by the PDGFRB (also known as IBGC4, IMF1, PDGFR, PDGFR1) gene (Gene ID 5159) in human. PDGFR-1 is a tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB. PDGF receptors consist of extracellular domains with five immunoglobulin (Ig) - like domains and intracellular parts with kinase domains, which contain characteristic inserts of about 100 amino acid residues without homology to kinases. Ligand binding occurs mainly to Ig-like domains 2 and 3, which causes dimerization of the receptor, which is further stabilized by direct receptor-receptor interactions involving Ig-like domain 4. In the absence of a bound ligand, receptor is present in an inactive conformation. However, upon ligand binding it undergoes dimerization and autophosphorylation on tyrosine residues. PDGFR-1m plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis, and migration. It is also considered to be essential for endothelial cell proliferation, migration and recruitment of pericytes and smooth muscle cells to form blood vessels. PDGFR-1 phosphorylates phospholipase C-gamma 1 (PLCG1), PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of diacylglycerol and IP3 that are involved in calcium mobilization and activation of PKC. Ref.: Heldin C-H (2013). Cell Commun. Signaling 11:97.C1

~180 kDa observed. Target band size appears larger than the calculated molecular weight of 120.6/119.6 kDa (human/mouse; signal peptide removed) due to glycosylation. Uncharacterized bands may be observed in some lysate(s).

KLH-conjugated linear peptide corresponding to a cytoplasmic sequence C-terminal to the kinase domain of human PDGFR .

Concentration: Please refer to lot specific datasheet.

Replaces: 06-498

Affinity purified.

Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.