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Purified Mouse Anti-Human CD140b
Purified Mouse Anti-Human CD140b

Western blot analysis of CD140b on a Hs68 cell lysate (Human skin fibroblasts; ATCC CRL-1635).  Lane 1: 1:50, lane 2: 1:100, lane 3: 1:200 dilution of the mouse anti-CD140b antibody. CD140b (PDGF Receptor β) may be observable as a band migrating at ~ 180 kDa.

Western blot analysis of CD140b on a Hs68 cell lysate (Human skin fibroblasts; ATCC CRL-1635).  Lane 1: 1:50, lane 2: 1:100, lane 3: 1:200 dilution of the mouse anti-CD140b antibody. CD140b (PDGF Receptor β) may be observable as a band migrating at ~ 180 kDa.

Product Details
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BD Transduction Laboratories™
PDGF Receptor β
Human (QC Testing)
Mouse IgG2b
Human PDGF Receptor β aa. 1-187
Western blot (Routinely Tested), Immunofluorescence, Immunohistochemistry (Tested During Development), Immunoprecipitation (Not Recommended)
180 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Western blot:  Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
610113 Rev. 1
Antibody Details
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28/CD140b

Platelet-derived growth factor (PDGF) is a potent mitogen for cells of esenchymal origin and exerts its effects by binding to the PDGF receptor (PDGFR), a  transmembrane protein tyrosine kinase. Both PDGF and PDGFR consist of subunits that form homo- or heterodimers with varying specificities: PDGF-AA binds only to αα PDGFR, PDGF-AB binds to both αα and αβ PDGFR, and  PDGF-BB binds to all three PDGFRs. Ligand binding induces phosphorylation and activation of the receptor and, in turn, initiation of an intracellular phosphorylation cascade. PDGFR localizes primarily to membrane invaginations termed caveolae, compartments that are enriched in several of its downstream effectors, including PI3 kinase, Shc, NCK, and PTP1D. Additionally, the β subunit of PDGFR has been implicated in cellular transformation. This effect is mediated by a C-terminal region of PDGFRβ and depends on pathways that involve either PLCβ or PI3 kinase.

610113 Rev. 1
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
610113 Rev.1
Citations & References
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Development References (5)

  1. Hansen K, Johnell M, Siegbahn A. Mutation of a Src phosphorylation site in the PDGF beta-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J. 1996; 1(19):5299-5313. (Biology). View Reference
  2. Liu J, Oh P, Horner T, Rogers RA, Schnitzer JE. Organized endothelial cell surface signal transduction in caveolae distinct from glycosylphosphatidylinositol-anchored protein microdomains. J Biol Chem. 1997; 272(11):7211-7222. (Biology). View Reference
  3. Liu P, Ying Y, Ko YG, Anderson RG. Localization of platelet-derived growth factor-stimulated phosphorylation cascade to caveolae. J Biol Chem. 1996; 271(17):10299-10303. (Biology). View Reference
  4. Mahboubi K, Pober JS. Activation of signal transducer and activator of transcription 1 (STAT1) is not sufficient for the induction of STAT1-dependent genes in endothelial cells. Comparison of interferon-gamma and oncostatin M. J Biol Chem. 2002; 277(10):8012-8021. (Biology: Immunofluorescence, Western blot). View Reference
  5. Shu L, Lee L, Shayman JA. Regulation of phospholipase C-gamma activity by glycosphingolipids. J Biol Chem. 2002; 277(21):18447-18453. (Biology: Western blot). View Reference
View All (5) View Less
610113 Rev. 1

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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.