Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Informationen zur Lagerung
Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze. The antibody was conjugated with R-PE under optimum conditions, and unconjugated antibody and free PE were removed.
Miura-Shimura, Duan, Rao, Reddi, Shimura, Rottapel, Druker, Tsygankov, Band, Band: "Cbl-mediated ubiquitinylation and negative regulation of Vav." in: The Journal of biological chemistry, Vol. 278, Issue 40, pp. 38495-504, (2003) (PubMed).
Thien, Langdon: "Cbl: many adaptations to regulate protein tyrosine kinases." in: Nature reviews. Molecular cell biology, Vol. 2, Issue 4, pp. 294-307, (2001) (PubMed).
Tsygankov, Teckchandani, Feshchenko, Swaminathan: "Beyond the RING: CBL proteins as multivalent adapters." in: Oncogene, Vol. 20, Issue 44, pp. 6382-402, (2001) (PubMed).
Cbl (Casitas B-lineage lymphoma) was identified in the genome of a transforming retrovirus from a mouse pre-B lymphoma. The cellular gene product c-Cbl is one of numerous Cbl-related proteins found in vertebrate and invertebrate organisms. It is an 120-kDa adapter protein that contains multiple functional domains, including a RING finger motif, a tyrosine kinase-binding (TKB) domain, and a proline-rich region. The TKB domain directly interacts with specific auto-phosphorylation sites in activated protein-tyrosine kinases (PTK). Through the RING finger motif, c-Cbl recruits and activates an E2 ubiquitin-conjugating enzyme, thus targeting the activated PTK for protein degradation. The proline-rich region contains SH3 domain-binding and 14-3-3 protein-binding motifs. c-Cbl is also phosphorylated at tyrosines 700 (Y700), 731, and 774 by Syk- and Src-family kinases after the stimulation of some integrins and a wide variety of receptors for antigens, immunoglobulins, growth factors, cytokines, and hormones. In turn, the phosphorylated Y700 site interacts with the SH2 domains of CRK and Vav1. The c-Cbl adapter protein is expressed in the cytoplasm in all tissues, with especially high levels of expression in hematopoietic cells. Through its many functional sites, c-Cbl plays key roles in the positive and negative regulation of vital cell functions, including T Cell Receptor-mediated cellular immune responses. The 47/c-Cbl monoclonal antibody recognizes the Y700-phosphorylated form of human c-Cbl. The orthologous phosphorylation site in mouse c-Cbl is Y698.