Recombinant Human Integrin alpha E beta 7 Protein, CF Summary
alpha E |
(Phe19-Ser1124 (Ile477Val & Arg482Gln))
Accession # P38570
|GGGSGGGS||Acidic Tail||6-His tag|
|Human Integrin beta 7 |
Accession # P26010
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 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.
Background: Integrin alpha E beta 7
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).
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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.
Why are there two point mutations (Ile477Val & Arg482Gln) in the Human Integrin alpha E subunit of Recombinant Human Integrin alpha E beta 7 Protein, CF (catalog # 5850-A3)?
These point mutations are natural variants that have been identified in the literature. As shown by our bioassay, the protein retains its ability to bind Human E-cadherin.
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