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Rabbit anti Human bcl 10 (NT) (CipER, CLAP)

Catalogue number: X1119P


Product Type Polyclonal Antibody
Units100 µg
Species reactivity Human
Application Western Blot
Product Form

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 herpesvirus-2 E-10 gene. Overexpression of Bcl10 induces JNK, p38, and NF- B 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).

Positive Control
Raji whole cell lysate

Synthetic peptide corresponding to amino acids 5 to 19 of the human BCL-10 protein.

Purification Method
Antigen Immunoaffiinity Purification

See vial for concentration

Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative

Functional Analysis
Western Blotting

Detects BCL10 by Western blot at 1 µg/ml. Detects a 31 kDa band in Raji whole cell lysate. Optimal concentration should be evaluated by serial dilutions.

Product should be stored at -20ºC. Aliquot to avoid freeze/thaw cycles

Ship Conditions
Ship at ambient temperature, freeze upon arrival

Product Stability
Products are stable for one year from purchase when stored properly

1. Willis, T.G., et al. Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. Cell 1999, 96, 35-45 2. Koseki, T., et al. CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10. J. Biol. Chem. 1999, 274, 9955-61 3. Yan, M., et al., mE10, a novel caspase recruitment domain-containing proapoptotic molecule. J. Biol. Chem. 1999, 274, 10287-92 4. Thome, M., et al., Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase. J. Biol. Chem. 1999, 274, 9962-8 5. Zhang, Q., et al., Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32). Nat. Genet. 1999, 22, 63-8 6. Srinivasula, S.M., et al., CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis. J. Biol. Chem. 1999, 274, 17946-54

This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.

Safety Datasheet(s) for this product:

Sodium Azide

Rabbit anti Human bcl 10 (NT) (CipER, CLAP)



Contact us

Exalpha Biologicals, Inc.
2 Shaker Road, Unit B101
Shirley, MA 01464
Phone: 978-425-1370