"ADAM17" Related Products

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Recombinant Human ADAM Metallopeptidase Domain 17, His-tagged

Cat. No.: ADAM17-592H
Product Overview: Recombinant human glycosylated catalytic domain (aa Pro1-Val477) of ADAM17/TACE secreted as mature, active enzyme frominsect cells,and purified using a C-terminal His-tag, 36kDa.
Description: ADAM17/TACE is a soluble or membrane-bound metalloproteinase primarily responsible for activation of proTNF-α, while also targeting proteins such as fractalkine, amyloid precursor proteins, and CD40. ADAM17/TACE is involved in cancer, vascular disorders, and inflammatory diseases such as rheumatoid arthritis and focal ischemic injury. The catalytic domain of ADAM17/TACE is able to cleave proTNF-α and can be used in inhibitor screening.
Source: insect cells.
Concentration: 0.45 µg/µl.
Purity: ≥90% (SDS-PAGE).
Formulation: Liquid. In 22.5mM TRIS, pH 7.5, containing 4.5µM ZnCl2, 0.0045% Brij-35 and 10% glycerol.
Specific Activity:: 2'430 U/µg enzyme. One unit will hydrolyze one pmole Mca-PLAQAV-Dpa-RSSSR-NH2 substrate (10µM) per minute at 37°C, in 25mM TRIS, pH 9.0.
Application: Study enzyme kinetics, cleave target substrates, screen inhibitors.
Storage: Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Pathways: Alzheimer"s disease; Epithelial cell signaling in Helicobacter pylori infection; Notch signaling pathway; Signaling by EGFR; Signalling by NGF
Gene Name: ADAM17 ADAM metallopeptidase domain 17 [ Homo sapiens ]
Synonyms: ADAM metallopeptidase domain 17; CSVP; TACE; ADAM18; CD156B; MGC71942; ADAM17; disintegrin and metalloproteinase domain-containing protein 17; ADAM 17; EC 3.4.24.86; TNF-alpha convertase; snake venom-like protease; TNF-alpha converting enzyme; TNF-alpha-converting enzyme; ADAM metallopeptidase domain 18;tumor necrosis factor, alpha, converting enzyme; a disintegrin and metalloprotease domain 17; CD156b antigen
Gene ID: 6668
mRNA Refseq: NM_003183
Protein Refseq: NP_003174
MIM: 603639
UniProt ID: P78536
Chromosome Location: 2p25
Function: PDZ domain binding; SH3 domain binding; integrin binding; interleukin-6 receptor binding; metal ion binding; metalloendopeptidase activity; metalloendopeptidase activity; metallopeptidase activity; peptidase activity; protein binding; zinc ion binding

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