Bcl-10 / Unconjugated /
Product Details
| Description | Apoptosis is related to many diseases including cancer. Cell death signals are transduced by death domain (DD) and caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. CARD containing cell death regulators include ARC, RAIDD, Apaf-1, caspase-9, and caspase-2. A novel CARD containing protein was recently identified by several groups and designated Bcl10, CIPER, mE10, CARMEN, CLAP. Bcl10 is a cellular homolog of the equine herpesvirus-2 E-10 gene. | |
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| Conjugate | Unconjugated | |
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| Target Species | Human, Mouse, Rat | |
| Applications | IHC-P, ICC, WB | |
| Supplier | Aviva Systems Biology | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About Bcl-10
This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]
This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2016]
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