Recombinant Mouse Integrin alpha 2 beta 1 Protein, CF 50 UG

• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When bovine collagen-II is coated at 10 μg/mL, Recombinant Mouse Integrin alpha 2 beta 1 binds with an apparent K    _D <1nM.  

• Source

  Chinese Hamster Ovary cell line, CHO-derived

  Mouse Integrin alpha 2 (Tyr27-Thr1129) Accession # Q62469.2	His-Pro	GGGSGGGS	Acidic Tail	HHHHHH
  Mouse Integrin beta 1 (Gln21-Asp728) Accession # P09055	His-Pro	GGGSGGGS	Basic Tail
  N-terminus				C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Tyr27 (Integrin  alpha 2) & Gln21 predicted: No results obtained, sequencing might be blocked (Integrin beta 1)

• Structure / Form

  Noncovalently-linked heterodimer

• Predicted Molecular Mass

  130 kDa (Integrin  alpha 2) & 86.5 kDa (Integrin beta 1)

• SDS-PAGE

  120-160 kDa, reducing conditions

Background: Integrin alpha 2 beta 1

Integrin alpha 2 beta 1 is one of twelve integrin family adhesion receptors that share the beta 1 subunit (1‑3). It is the non‑covalent heterodimer of 160 kDa alpha 2 (CD49b) and 130 kDa beta 1 (CD29) type I transmembrane glycoprotein subunits. It is one of six very late antigens on activated T cells, designated VLA2 (3). The alpha 2 extracellular domain (ECD) contains an I (inserted) domain which includes the ligand binding site (2, 3). The beta 1 ECD contains a vWFA domain, which participates in binding. Each subunit then has a transmembrane sequence and a short cytoplasmic tail. The dimer is folded when it is least active. Divalent cations and intracellular (inside‑out) signaling convert it to its most active, extended and open conformation (1, 2). The 1103 amino acid (aa) mouse alpha 2 extracellular domain (ECD) shares 93% aa sequence identity with rat and  80‑81% with human, canine, bovine and equine alpha 2, while the 708 aa mouse beta 1 ECD shares 98% aa identity with rat and 93-94% with human, bovine, porcine, ovine, canine and feline beta 1. The I domain‑containing beta 1 integrins ( alpha 1 beta 1, alpha 2 beta 1, alpha 10 beta 1 and alpha 11 beta 1) all bind collagens, with alpha 2 beta 1 preferring collagens I‑III (4, 5). Platelet alpha 2 beta 1, also called GPIa, cooperates with another adhesion protein, GPVI, to coordinate platelet collagen binding and activation (3, 6, 7). Other alpha 2 beta 1 ligands include laminin, decorin, E‑cadherin, and collagen‑like regions of collectin molecules such as C1q (4). Adhesion is synergized by crosstalk with syndecan‑1 or HGF R/c‑Met, and antagonized by crosstalk with integrin alpha 1 beta 1 (8‑10). In addition to expression on selected hematopoietic cells, alpha 2 beta 1 is present on a wide variety of non‑hematopoietic cells (4). Mice deficient in the alpha 2 subunit have defects in innate immune responses, wound mast cell infiltration and angiogenesis, and platelet responses to collagen (6, 11, 12). In innate immunity, alpha 2 beta 1 binding to C1q initiates the complement cascade and co‑stimulates mast cell activation, triggering neutrophil influx (4, 12).

• References:

1. Takada, Y. et al. (2007) Genome Biol. 8:215.

2. Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.

3. Takada, Y. and M.E. Hemler (1989) J. Cell Biol. 109:397.

4. Zutter, M.M. and B.T Edelson (2007) Immunobiology 212:343.

5. McCall-Culbreath, K.D. and M.M. Zutter (2008) Curr. Drug Targets 9:139.

6. Sarratt, K.L. et al. (2005) Blood 106:1268.

7. Lecut, C. et al. (2005) Thromb. Haemost. 94:107.

8. Vuoriluoto, K. et al. (2008) Exp. Cell Res. 314:3369.

9. McCall-Culbreath, K.D. et al. (2008) Blood 111:3562.

10. Abair, T.D. et al. (2008) Exp. Cell Res. 314:3593.

11. Zweers, M. et al. (2006) J. Invest. Dermatol. 127:467.

12. Edelson, B.T. et al. 2006) Blood 107:143.

• Entrez Gene IDs:

  3673 (Human); 16401 (Mouse)

• Alternate Names:

  Integrin alpha 2 beta 1