Bcl 10, NT, Blocking Peptide (CIPER, mE10, CARMEN, CLAP), Purified

Peptide corresponding to amino acids 5 to 19 of human origin (1-6). 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 (1-6). Bcl10 is a cellular homolog of the equine Herpes virus-2 E-10 gene. Overexpression of Bcl10 induces JNK, p38, and NF-kB activation (1,2,4,6). Bcl10 interacts with caspase-9 and enhances pro-caspase-9 processing (3) and induces apoptosis through caspase-9 activation (3.6). BCL10 exhibits a variety of mutations in MALT lymphomas and in B and T cell lineage lymphomas indicating that it may be commonly involved in the pathogenesis of human malignancy (1,5). BCL10 is expressed in many human and murine tissues and cell lines (2-6). , Bcl 10 is identi?ed through its direct involvement in t(1,14)(p22,q32) of mucosa-associated lymphoid tissue (MALT) lymphoma. It is also expressed both in normal lymphoid tissue but doesn't exhibit crossreactivity with other tissues except breast. In non-malignant B-cell follicles the protein is expressed in the cytoplasm of the germinal center B-cells, while in MALT lymphomas with t(1,14)(p22,q32), Bcl 10 expression can be detected both in nucleus and cytoplasm. Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Reconstitute to nominal volume by adding sterile 40-50% glycerol and store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.