Recombinant Mouse Integrin alpha E beta 7 Protein, CF
Recombinant Mouse Integrin alpha E beta 7 Protein, CF Summary
Product Specifications
| Mouse Integrin alpha E (Phe20-Arg1113, Ser453Gly) Accession # ABD49099 |
His-Pro | GGGSGGGS | Acidic Tail | 6-His tag |
| Mouse Integrin beta 7 (Glu20-Arg724) Accession # P26011 |
GGGSGGGS | Basic Tail | ||
| N-terminus | C-terminus | |||
Analysis
Product Datasheets
Carrier Free
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.
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.
8356-A3
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 500 μg/mL in sterile 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.
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Reconstitution Calculator
Background: Integrin alpha E beta 7
Integrin alpha E beta 7 (also called M290 in mouse and HML-1 in human) is a type I transmembrane adhesion protein. It is composed of an alpha E subunit (epithelial-associated; also designated as CD103) which is expressed as disulfide-linked 150 kDa and 25 kDa heavy and light chains, and a non-covalently associated 130 kDa beta 7 glycoprotein subunit (1, 2). Each subunit has a transmembrane sequence and a short cytoplasmic tail. Integrin alpha E beta 7 is the only known integrin family receptor containing the alpha E subunit, while the beta 7 subunit is also a component of Integrin alpha 4 beta 7 (1-3). The alpha E extracellular domain (ECD) contains 7 beta -propeller domains surrounding an I domain followed by domains called tight, calf-1 and calf-2. An extra X domain, not found in any other alpha integrin, is also present and contains a proteolytic cleavage site (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, E-Cadherin (4). The 1093 amino acid (aa) mouse alpha E extracellular domain shares 79% and 99% aa sequence identity with human and rat alpha E respectively, while the 704 aa mouse beta 7 ECD shares 87% and 94% aa identity with human and rat beta 7, respectively. Integrin alpha E beta 7 is mainly restricted to mucosal tissues, where it engages E-Cadherin (4-6). It was first identified as a marker of intestinal intra-epithelial lymphocytes (1, 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 Integrin alpha E beta 7 in the days following their migration to epithelium in the intestines, lungs, and tonsils (6-13). In these tissues Integrin alpha E beta 7 facilitates immune surveillance, including the destruction of infected or transformed epithelial cells and the induction of T cell adaptive responses (7-13). Pathologically, Integrin alpha E beta 7 may be involved in allograft rejection of transplanted pancreatic islets and other tissues (14).
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- Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.
- Higgins, J.M.G. et al. (2000) J. Biol. Chem. 275:25652.
- Cepek, K.L. et al. (1994) Nature 372:190.
- Wagner, N. et al. (1996) Nature 382:366.
- Le Floc'h, A. et al. (2007) J. Exp. Med. 204:559.
- Smyth, L.J.C. et al. (2007) Clin. Exp. Immunol. 149:162.
- Woodberry, T. et al. (2005) J. Immunol. 175:4355.
- Jaensson, E. et al. (2008) J. Exp. Med. 205:2139.
- del Rio, M.-L. et al. (2008) J. Immunol. 181:6178.
- Sung, S.J. et al. (2006) J. Immunol. 176:2161.
- Siewert, C. et al. (2008) J. Immunol. 180:146.
- Feng, Y. et al. (2002) J. Exp. Med. 196:877.
FAQs
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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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