Recombinant Mouse Integrin alpha 11 beta 1 Protein, CF

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Recombinant Mouse Integrin alpha 11 beta 1 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Collagen I is coated at 10 μg/mL, Recombinant Mouse Integrin alpha 11 beta 1 binds with an apparent KD <20 nM.
Chinese Hamster Ovary cell line, CHO-derived mouse Integrin alpha 11 beta 1 protein
Mouse Integrin alpha 11
Accession # P61622
Mouse Integrin beta 1
Accession # P09055
N-terminus C-terminus
N-terminal Sequence
Phe23 ( alpha 11 subunit) & Gln21 predicted: No results obtained, sequencing might be blocked ( beta 1 subunit)
Structure / Form
Noncovalently-linked heterodimer
Predicted Molecular Mass
134 kDa ( alpha 11 subunit) & 86.5 kDa ( beta 1 subunit)
115-135 kDa & 155-175 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 300 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Integrin alpha 11 beta 1

Integrin alpha 11 beta 1 is a noncovalent heterodimeric collagen receptor that contains a 150 kDa alpha 11 subunit complexed to a 130 kDa beta 1/CD29 subunit.  alpha 11 beta 1 is the only known alpha 11-containing integrin. By contrast, at least twelve alpha -integrins share the beta 1 subunit (1-5). alpha 11 beta 1 is expressed on fibroblasts from cornea, skin and periodontal ligament (3-9). It is also expressed on mesenchymal stem cells and is considered a marker for non-muscle mesenchymal tissue (3, 8-10). Expression of alpha 11 beta 1 is stimulated by TGF-beta 1, activin A, and type I interferons, and down‑regulated by FGF-2 (6, 9-11). The alpha 11 extracellular domain (ECD) contains a vWFA domain which includes the ligand binding site (2-5). The beta 1 ECD also contains a vWFA domain, which participates in binding. Each subunit has a transmembrane sequence and a short cytoplasmic tail. The dimer assumes a folded configuration at "rest". Divalent cations and intracellular (inside-out) signaling convert it to an active, extended and open conformation (1, 2). The 1119 amino acid (aa) mouse alpha 11 ECD shares 90% and 95% aa sequence identity with rat and human alpha 11, respectively, while the 708 aa mouse beta 1 ECD shares 98% aa identity with rat and 93-94% aa identity with human, bovine, porcine, ovine, canine and feline beta 1. 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 (3-5). alpha 11 beta 1 preferentially binds interstitial collagens such as type I (5, 8, 12). It can contract collagen matrices and influence inflammatory edema (3, 13). Depending on context, alpha 11 beta 1 can support or inhibit cell migration on collagen (7, 8). It is frequently up‑regulated in the stroma of lung adenocarcinomas and enhances tumorigenicity (14, 15). alpha 11 beta 1 is also involved in myofibroblast differentiation in human corneal fibroblasts and human cardiac fibroblasts (9, 16).

  1. Takada, Y. et al. (2007) Genome Biol. 8:215.
  2. Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.
  3. Popova, S.N. et al. (2007) Acta Physiol. 190:179.
  4. Lehnert, K. et al. (1999) Genomics 60:179.
  5. Velling, T. et al. (1999) J. Biol. Chem. 274:25735.
  6. Gouttenoire, J. et al. (2010) Eur. J. Cell Biol. 89:307.
  7. Popova, S.N. et al. (2004) Dev. Biol. 270:427.
  8. Tiger, C-F. et al. (2001) Dev. Biol. 237:116.
  9. Carrecedo, S. et al. (2010) J. Biol. Chem. 285:10434.
  10. Varas, L. et al. (2007) Stem Cells Dev. 16:965.
  11. Coelho, L.F.L. et al. (2006) Cytokine 33:352.
  12. Zhang, W-M. et al. (2003) J. Biol. Chem. 278:7270.
  13. Svendsen, O.S. et al. (2009) Arterioscler. Thromb. Vasc. Biol. 29:1864.
  14. Wang, K-K. et al. (2002) Oncogene 21:7598.
  15. Zhu, C-Q. et al. (2007) Proc. Natl. Acad. Sci. USA 104:11754.
  16. Talior-Volodarsky, I. et al. (2012) Cardiovasc. Res. 96:265.
Alternate Names
Integrin alpha 11 beta 1


  1. What is the amino acid sequence of the acidic and basic tails?

    • Acidic and basic tails are added to the protein to help facilitate optimal activity. While we generally include sequence information on the product datasheet, the sequences of these tails are considered confidential information.

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