CBL / Unconjugated /

Product Details

Description	The mammalian cbl family of ubiquitin ligases consists of three homologs known as cbl (also known as c-Cbl), Cbl-B, and Cbl-3 which share highly conserved a tyrosine-kinase-binding domain, linker and RING finger domain in their amino-terminal halves. Similar to other E3 ubiquitin ligases, Cbl catalyzes the transfer of ubiquitin from an E2 or Ubc (ubiquitin-conjugating) enzyme to the e-amino group of a lysine residue of the substrate protein. Cbl acts to negatively regulate many types of cell-surface receptors, including the Syk protein tyrosine kinase family. Cbl is thought to be involved in T- and B-cell signaling, in addition to thymus development. Of the three known homologs in the cbl family, cbl antibody reacts specifically with cbl. Multiple isoforms of cbl have been reported.
Conjugate	Unconjugated
Clone
Target Species	Human, Mouse, Rat
Applications	ELISA, IF, WB
Supplier	Aviva Systems Biology
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About CBL
This gene is a proto-oncogene that encodes a RING finger E3 ubiquitin ligase. The encoded protein is one of the enzymes required for targeting substrates for degradation by the proteasome. This protein mediates the transfer of ubiquitin from ubiquitin conjugating enzymes (E2) to specific substrates. This protein also contains an N-terminal phosphotyrosine binding domain that allows it to interact with numerous tyrosine-phosphorylated substrates and target them for proteasome degradation. As such it functions as a negative regulator of many signal transduction pathways. This gene has been found to be mutated or translocated in many cancers including acute myeloid leukaemia, and expansion of CGG repeats in the 5' UTR has been associated with Jacobsen syndrome. Mutations in this gene are also the cause of Noonan syndrome-like disorder. [provided by RefSeq, Jul 2016]

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