ADAM 10, CT, Blocking Peptide (Kuzbanian, KUZ, MADM, a Disintegrin and Metalloprotease)

Peptide corresponding to amino acids 732 to 748 of human ADAM10 (1). This sequence is identical to those of bovine and rat origins and differs from that of mouse ADAM10 by one amino acid (2,4).\nProinflammatory cytokine tumor necrosis factor-a (TNF-a) contributes to a variety of inflammatory responses and programmed cell death. Notch receptor and its ligand participate in cell fate decisions during vertebrate development and are associated with several human disorders, including a T-cell lymphoma. TNF-a, notch and its ligand delta are all membrane-bond molecules, which are cleaved by proteases to release mature proteins or functional receptor. ADAM10, a metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease), was recently identified to cleave TNF-a, notch and its ligand delta (1-3). The genes encoding human, mouse, and bovine ADAM10 were recently cloned and designated ADAM 10, kuzbanian (KUZ), and MADM, respectively, (1,2,4). ADAM10 mRNA is expressed in a variety of human and bovine tissues (1,4). SOURCE: Rabbit anti-ADAM10 (CT) polyclonal antibody was raised against a peptide corresponding to amino acids 732 to 748 of human ADAM10 (1). This sequence is identical to those of bovine and rat origins and differs from that of mouse ADAM10 by one amino acid (2,4).

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SPECIFICATIONS

Catalog Number

A0859P

Size

50ug

Form

Supplied as a lyophilized powder.

Purity

Purified 60-70%

References

1. Rosendahl MS, Ko SC, Long DL, et al. Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. J Biol Chem 1997;272:24588-93 2. Pan D, Rubin GM. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 1997;90:271-80 3. Qi H, Rand MD, Wu X, Sestan N, Wang W, Rakic P, Xu T, Artavanis-Tsakonas S. Processing of the notch ligand delta by the metalloprotease Kuzbanian. Science 1999;283:91-4 4. Howard L, Lu X, Mitchell S, Griffiths S, Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem J 1996;317:45-50