Human Integrin alpha 3/CD49c Alexa Fluor® 750-conjugated Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Example

Detection of Integrin alpha 3/CD49c in HT1080 Human Cell Line by Flow Cytometry. HT1080 human fibrosarcoma cell line was stained with Mouse Anti-Human Integrin alpha 3/CD49c Alexa Fluor® 750-conjugated Monoclonal Antibody (Catalog # FAB1345S, filled histogram) or isotype control antibody (Catalog # IC002S, open histogram). View our protocol for Staining Membrane-associated Proteins.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: Integrin alpha 3/CD49c
VLA-3 (Very Late Antigen 3) is a member of the integrin family, beta 1 subfamily, of cell membrane adhesion molecules (1-3). Integrins are nondisulfide-linked transmembrane (TM) heterodimers that contain an alpha - and beta -subunit (1). VLA-3 is composed of an alpha 3 and beta 1 subunit. The alpha 3/CD49c subunit is a 130-150 kDa type I TM glycoprotein. It only associates with the beta 1 integrin subunit. It is synthesized as a 1051 amino acid (aa) precursor that undergoes proteolytic cleavage to generate a disulfide-linked 110 kDa, 843 aa extracellular heavy chain and a 30 kDa, 176 aa TM/cytoplasmic light chain (1, 4, 5, 6). The heavy chain contains seven 60 aa repeats that fold into a propeller-like structure (7). Sequences involving the first three repeats are associated with ligand binding (1). The light chain has two cytoplasmic alternate splice forms. The A form cytoplasmic domain is 52 aa, while the B form cytoplasmic domain is 37 aa (5). Human alpha 3 heavy chain is 88% aa identical to mouse heavy chain. VLA-3 is known to bind fibronectin, collagen, and laminin-1, 5, 8, 10 and 11 (1). It also binds tetraspanins such as CD9, CD63 and CD151. CD151 binding may actually stabilize VLA-3, enabling it to bind to additional factors (8).
- Tsuji, T. et al. (2004) J. Membr. Biol. 200:115.
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- Kreidberg, J.A. (2000) Curr. Opin. Cell Biol. 12:548.
- Takada, Y. et al. (1991) J. Cell. Biol. 115:257.
- de Melker, A.A. et al. (1997) Lab. Invest. 76:547.
- Krokhin, O.V. et al. (2003) Biochemistry 42:12950.
- Springer, T.A. (2002) Curr. Opin. Struct. Biol. 12:802.
- Nishiuchi, R. et al. (2005) Proc. Natl. Acad. Sci. USA 102:1939.
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