Bcl-10 / Biotin / BL10/411
Product Details
Description | BCL10, with an N-terminal caspase recruitment domain (CARD), is found in a number of apoptotic regulatory molecules. It was identified through its direct involvement in t(1;14) of mucosa-associated lymphoid tissue (MALT) lymphoma. Expression of BCL10 was shown to induce NFKB activation in a NIK-dependent pathway. This MAb labels subpopulations of normal B and T cells and is a useful tool for the sub-classification of lymphomas. In MALT lymphomas with the t(1;14) translocation, while 55% of MALT lymphomas lacking this translocation exhibited the same labeling pattern, although at a much lower level. | |
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Conjugate | Biotin | |
Clone | BL10/411 | |
Target Species | Human | |
Applications | ELISA | |
Supplier | Novus Biologicals | |
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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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