Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H||FC, IP||M||Purified||Monoclonal Antibody|
|Presentation||Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at 2-8°C from date of receipt.|
|Material Size||100 µL|
|Anti-human CD15, clone TS151 - 2425993||2425993|
|Anti-human CD15, clone TS151 - 2446289||2446289|
|Anti-human CD15, clone TS151 - 2068459||2068459|
|Anti-human CD151 clone TS151 - NRG1844839||NRG1844839|
|Anti-human CD151, clone TS151 -2822542||2822542|
|Reference overview||Pub Med ID|
|Multiple levels of interactions within the tetraspanin web. |
Charrin, Stéphanie, et al.
Biochem. Biophys. Res. Commun., 304: 107-12 (2003) 2003
The tetraspanin web refers to a network of molecular interactions involving tetraspanins and other molecules. Inside the tetraspanin web, small primary complexes containing only one tetraspanin and one specific partner molecule such as CD151/alpha3beta1 integrin and CD9/CD9P-1 (FPRP) can be observed under particular conditions. Here we demonstrate that when cells are lysed with Brij97, the tetraspanins CD151 and CD9 allow and/or stabilize the interaction of their partner molecules with other tetraspanins and that their two partners associate under conditions maintaining tetraspanin/tetraspanin interactions. The tetraspanins were also found to partition into a detergent-resistant membrane environment to which the integrin alpha3beta1 was relocalized upon expression of CD151.
|The major CD9 and CD81 molecular partner. Identification and characterization of the complexes. |
Charrin, S, et al.
J. Biol. Chem., 276: 14329-37 (2001) 2001
By associating with specific partner molecules and with each other, the tetraspanins are thought to assemble multimolecular complexes that may be especially relevant with respect to metastasis. We have previously identified a 135-kDa molecule (CD9P-1) as a major molecular partner of CD9 in cancer cell lines. This molecule was identified, after immunoaffinity purification and mass spectrometry analysis, as the protein encoded by the KIAA1436 gene and the human ortholog of a rat protein known as FPRP. Cross-linking experiments detected a complex of the size of CD9 plus CD9P-1, showing that these glycoproteins directly associate with each other, probably in the absence of any other molecule. The use of chimeric CD9/CD82 molecules revealed the role of the second half of CD9, comprising the large extracellular loop and the fourth transmembrane domain. CD9P-1 was also shown to form separate complexes with CD81 and with an unidentified 175-kDa molecule. It also associated with other tetraspanins under conditions maintaining tetraspanin/tetraspanin interactions. The identification of a protein strongly linked to the tetraspanin web and the production of a specific monoclonal antibody will help to further characterize the role of this "web" under physiological and pathological conditions.