Recombinant Mouse Integrin alpha 11 beta 1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Integrin alpha 11 beta 1 Protein, CF Summary

Details of Functionality
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.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Integrin alpha 11 beta 1 protein
Mouse Integrin alpha 11
(Phe23-Pro1141)
Accession # P61622
HP GGGSGGGS Acidic Tail HHHHHH
Mouse Integrin beta 1
(Gln21-Asp728)
Accession # P09055
HP GGGSGGGS Basic Tail
N-terminus C-terminus
Accession #
N-terminal Sequence
Phe23 ( alpha 11 subunit) & Gln21 predicted: No results obtained, sequencing might be blocked ( beta 1 subunit)
Structure / Form
Noncovalently-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
134 kDa ( alpha 11 subunit) & 86.5 kDa ( beta 1 subunit).
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.
SDS-PAGE
115-135 kDa & 155-175 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 300 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Integrin alpha 11 beta 1 Protein, CF

  • Integrin alpha 11 beta 1

Background

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.

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