Recombinant Human Integrin alpha E beta 7 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human Integrin alpha E beta 7 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When rhE-Cadherin is coated at 2 μg/mL, rhIntegrin alpha E beta 7 binds with an apparent Kd <5 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha E beta 7 protein
Human Integrin alpha E
(Phe19-Ser1124 (Ile477Val & Arg482Gln))
Accession # P38570
GGGSGGGSAcidic Tail 6-His tag
Human Integrin beta 7
(Glu20-His723)
Accession # P26010
His-ProGGGSGGGSBasic Tail
N-terminus C-terminus
Accession #
N-terminal Sequence
Phe19 ( alpha E) & Glu20 ( beta 7)
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

Dilutions
  • Binding Activity
Theoretical MW
130.7 kDa ( alpha E) & 84.7 kDa ( beta 7).
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
150-170 kDa & 120-130 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 100 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 Human Integrin alpha E beta 7 Protein, CF

  • Integrin alpha E beta 7

Background

Integrin alpha E beta 7, also called HML-1 (human mucosal lymphocyte antigen), is the only known integrin family adhesion receptor containing the alpha E (epithelial-associated) subunit, and shares the beta 7 subunit with alpha 4 beta 7 (1-3). alpha E beta 7 is the non‑covalent multimer of alpha E (designated CD103), present as 150 kDa and 25 kDa heavy and light chains, and 130 kDa beta 7 type I transmembrane glycoprotein subunits (2, 3). The alpha E extracellular N-terminal beta -propeller structure contains X (which contains the cleavage site) and I domains, and is followed by domains called thigh, calf-1 and calf-2 (1, 2). The beta 7 ECD contains a vWFA domain, which interacts with the alpha E beta ‑propeller to form a binding domain. The MIDAS motif (metal ion‑dependent adhesion site) is critical for binding of alpha E beta 7 to its ligand (4). Each subunit has a transmembrane sequence and a short cytoplasmic tail. The 1105 aa human alpha E extracellular domain shares 70-79% aa sequence identity with mouse, rat, equine, bovine, canine and feline alpha E, while the 705 aa human beta 7 ECD shares 87%, 87%, 91% and 88% aa identity with mouse, rat, equine and bovine beta 7, respectively. alpha E beta 7 is mainly restricted to mucosal tissues, where it engages the epithelial adhesion molecule E-cadherin (4-6). It was first identified as a marker of intestinal intra-epithelial lymphocytes (2, 5, 6). It has since been recognized that a variety of leukocytes, such as cytotoxic CD8+ T cells, some dendritic cells, and effector/memory-like regulatory T cells, acquire alpha E beta 7 in the days following their migration to epithelial tissues such as the intestines, lungs, and epithelial layers of tonsils (6-13). In these tissues alpha E beta 7 facilitates immune surveillance, including destruction of infected or transformed epithelial cells and induction of T cell adaptive responses (7-13). Pathologically, alpha E beta 7 may be involved in allograft rejection of transplanted pancreatic islets and other tissues (14).

  1. Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.
  2. Shaw, S.K. et al. (1994) J. Biol. Chem. 269:6016.
  3. Erle, D.J. et al. (1991) J. Biol. Chem. 266:11009.
  4. Higgins, J.M.G. et al. (2000) J. Biol. Chem. 275:25652.
  5. Cepek, K.L. et al. (1994) Nature 372:190.
  6. Wagner, N. et al. (1996) Nature 382:366.
  7. Le Floc’h, A. et al. (2007) J. Exp. Med. 204:559.
  8. Smyth, L.J.C. et al. (2007) Clin. Exp. Immunol. 149:162.
  9. Woodberry, T. et al. (2005) J. Immunol. 175:4355.
  10. Jaensson, E. et al. (2008) J. Exp. Med. 205:2139.
  11. del Rio, M.-L. et al. (2008) J. Immunol. 181:6178.
  12. Sung, S.J. et al. (2006) J. Immunol. 176:2161.
  13. Siewert, C. et al. (2008) J. Immunol. 180:146.
  14. Feng, Y. et al. (2002) J. Exp. Med. 196:877.

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