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Purified Mouse Anti-Human CD49b
Purified Mouse Anti-Human CD49b

Western blot analysis of CD49b (Integrin α2) on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2). Lane 1; 1:250, lane 2: 1: 500, lane 3: 1; 1000 dilution of the anti-human CD49b antibody.

Purified Mouse Anti-Human CD49b

Immunofluorescence staining of WiDr cells (Human colorectal adenocarcinoma; ATCC CCL-218).

Western blot analysis of CD49b (Integrin α2) on a HeLa cell lysate (Human cervical epitheloid carcinoma; ATCC CCL-2.2). Lane 1; 1:250, lane 2: 1: 500, lane 3: 1; 1000 dilution of the anti-human CD49b antibody.

Immunofluorescence staining of WiDr cells (Human colorectal adenocarcinoma; ATCC CCL-218).

Product Details
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BD Transduction Laboratories™
Integrin α2; VLA-2α
Human (QC Testing)
Mouse IgG2a
Human VLA-2α aa.42-245
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
150 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

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

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to 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.
611016 Rev. 1
Antibody Details
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Integrins are a family of dimeric proteins that mediate cell-to-cell and extracellular matrix adhesion. They consist of a large α chain that is non-covalently associated with a smaller β chain which is used to define integrin subfamilies. These molecules exhibit a wide range of expression throughout development and adulthood. VLA-2 (very late antigen), a member of the integrin superfamily, was identified on activated T cells, but has since been reported to be on various cell types. VLA-2 is reported to be a heterodimer of integrin α2 (CD49b) and integrin β1 (CD29) subunits. The α2 chain contains a large extracellular domain, a transmembrane domain, and a short cytoplasmic tail. VLA-2 functions as a collagen receptor on platelets and fibroblasts, as well as a collagen and laminin receptor on endothelial and epithelial cells. On activated T cells, VLA-2, like LFA-1, exhibits increased number and affinity of ligand binding. Interactions of these molecules with their extracellular matrix ligands is important for directing effector T cells to their target tissues and to provide co-stimulatory signals. Thus, VLA-2 not only plays an important role in cellular adhesion, but may function in intracellular signal transmission.

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Format Details
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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.
611016 Rev.1
Citations & References
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Development References (5)

  1. Emsley J, King SL, Bergelson JM, Liddington RC. Crystal structure of the I domain from integrin alpha2beta1. J Biol Chem. 1997; 272(45):28512-28517. (Biology). View Reference
  2. Forster C, Makela S, Warri A. Involvement of estrogen receptor beta in terminal differentiation of mammary gland epithelium. Proc Natl Acad Sci U S A. 2002; 99(24):15578-15583. (Biology: Cell separation, Immunohistochemistry). View Reference
  3. Russell JS, Tofilon PJ. Radiation-induced activation of nuclear factor-kappaB involves selective degradation of plasma membrane-associated I(kappa)B(alpha). Mol Biol Cell. 2002; 13(10):3431-3440. (Biology: Western blot). View Reference
  4. Takada Y, Hemler ME. The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain. J Cell Biol. 1989; 109(1):397-407. (Biology). View Reference
  5. Wu JE, Santoro SA. Complex patterns of expression suggest extensive roles for the alpha 2 beta 1 integrin in murine development. Development. 1994; 199(4):292-314. (Biology). View Reference
View All (5) View Less
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Please refer to Support Documents for Quality Certificates

Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described

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.