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Anti-CD49e [SNAKA52]

Info

Catalogue Number 152486
Applications ELISA Fn
Antigen/Gene or Protein Targets Integrin alpha5 (CD49e)
Synonyms Integrin Subunit Alpha 5; Fibronectin Receptor Subunit Alpha; CD49 Antigen-Like Family Member E; Integrin Alpha-F; VLA-5; FNRA; Very Late Activation Protein 5; Alpha Subunit; Fibronectin Receptor; Alpha Polypeptide; Fibronectin Receptor; Alpha Subunit; Fibronectin Receptor; Alpha Polypeptide; Integrin Alpha; CD49e Antigen; CD49e; VLA5A
Reactivity Human
Relevance CD49e is the integrin alpha 5 chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 5 undergoes post translational cleavage in the extracellular domain to yield disulfide linked light and heavy chains that join with beta 1 to form a fibronectin receptor that is known variously: in lymphocytes as very late (activation) antigen 5 (VLA5); in platelets as glycoprotein IcIIa; and in fibroblasts as extracellular matrix receptor 6 (ECMVI). In addition to adhesion, integrins are known to participate in cell surface mediated signalling. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis.
Host Mouse
Immunogen α5β1 purified from human placenta.
Subclass IgG
Positive Control HeLa cells
Myeloma Used P3X63Ag8.653
Notes The binding of SNAKA52 is inhibited by anti-beta1 mAbs, indicating that its epitope is close to the interface between the alpha and beta subunits.
Research Area Adhesion, Apoptosis and Programmed Cell Death, Cell Signaling & Signal Transduction, Immunology

References: 6 entries

Clark et al. 2005. J Cell Sci. 118(Pt 2):291-300. PMID: 15615773.

A specific alpha5beta1-integrin conformation promotes directional integrin translocation and fibronectin matrix formation.

Europe PMC ID: 15615773

Mould et al. 2003. J Biol Chem. 278(19):17028-35. PMID: 12615914.

Conformational changes in the integrin beta A domain provide a mechanism for signal transduction via hybrid domain movement.

Europe PMC ID: 12615914

Fine mapping of inhibitory anti-alpha5 monoclonal antibody epitopes that differentially affect integrin-ligand binding.

Europe PMC ID: 10567237

Burrows et al. 1999. Biochem J. 344 Pt 2:527-33. PMID: 10567237.

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References: 6 entries

Clark et al. 2005. J Cell Sci. 118(Pt 2):291-300. PMID: 15615773.

A specific alpha5beta1-integrin conformation promotes directional integrin translocation and fibronectin matrix formation.

Europe PMC ID: 15615773

Mould et al. 2003. J Biol Chem. 278(19):17028-35. PMID: 12615914.

Conformational changes in the integrin beta A domain provide a mechanism for signal transduction via hybrid domain movement.

Europe PMC ID: 12615914

Fine mapping of inhibitory anti-alpha5 monoclonal antibody epitopes that differentially affect integrin-ligand binding.

Europe PMC ID: 10567237

Burrows et al. 1999. Biochem J. 344 Pt 2:527-33. PMID: 10567237.

Fn


Add a reference

References: 6 entries

Clark et al. 2005. J Cell Sci. 118(Pt 2):291-300. PMID: 15615773.

A specific alpha5beta1-integrin conformation promotes directional integrin translocation and fibronectin matrix formation.

Mould et al. 2003. J Biol Chem. 278(19):17028-35. PMID: 12615914.

Conformational changes in the integrin beta A domain provide a mechanism for signal transduction via hybrid domain movement.

Fine mapping of inhibitory anti-alpha5 monoclonal antibody epitopes that differentially affect integrin-ligand binding.

Burrows et al. 1999. Biochem J. 344 Pt 2:527-33. PMID: 10567237.

Fn


Add a reference


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