Phe33 (Integrin alpha 3) & No results obtained. Gln21 inferred from enzymatic pyroglutamate treatment revealing Thr22 (Integrin beta 1)
Structure / Form
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
116 kDa (Integrin alpha 3) & 86 kDa (Integrin beta 1). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
102-163 kDa, reducing conditions
Read Publication using 9374-A3 in the following applications:
Integrin alpha 3 beta 1,
also known as VLA-3 (Very Late Antigen 3), is a member of the integrin family,
beta 1 subfamily, of cell membrane adhesion molecules (1-3). It is a
non-covalent heterodimer composed of two type I transmembrane glycoprotein
subunits, a 130-150 kDa alpha 3 (CD49c) subunit and a 130-140 kDa beta 1 (CD29)
subunit. Integrin alpha 3 only associates with the beta 1 subunit. It is
synthesized as a 1051 amino acid (aa) precursor that undergoes proteolytic
cleavage to generate a disulfide-linked 110 kDa, 842 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). Mouse alpha 3 heavy chain is 88% aa identical to human heavy chain. Unlike
the alpha 3 subunit, the mouse beta 1 subunit does not undergo proteolytic
cleavage (8). The molecule contains a 708 aa extracellular region, a 23 aa TM
segment, and a 47 aa cytoplasmic domain. The extracellular region contains one
von Willebrand factor-like A domain and four cysteine-rich repeats. Mouse beta 1 extracellular domain shares 93% and 98% aa sequence identity with human and
rat beta 1, respectively. Integrin alpha 3 beta 1 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 it, enabling it to bind to additional factors (9).
Tsuji, T. et al. (2004) J. Membr. Biol. 200:115.
Gu, J. and N. Taniguchi (2004) Glycoconj. J. 21:9.
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.
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