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ADAM17 (catalytic domain) (human), (recombinant) (His-tag)

BML-SE268-0010 10 µg 538.00 USD
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Product Details

Alternative Name:TACE, A disintegrin and metalloproteinase 17, Tumor necrosis factor-α-converting enzyme

Recombinant glycosylated catalytic domain (aa Pro18-Val477) of ADAM17/TACE (A disintegrin and metalloproteinase 17; Tumor necrosis factor-α-converting enzyme), cloned from human cDNA (NM_003183), secreted as mature, active enzyme from insect cells, and purified using a C-terminal His-tag.

MW:~30.5kDa (calculated), ~36kDa doublet (SDS-PAGE)
Source:Produced in insect cells. Produced in a baculovirus expression system.
UniProt ID:P78536
Formulation:Liquid. In 22.5mM TRIS, pH 7.5, containing 4.5µM ZnCl2, 0.0045% Brij-35 and 10% glycerol.
Purity:≥90% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Specific Activity:≥1800 U/µg enzyme. One unit will hydrolyze one pmole Mca-PLAQAV-Dpa-RSSSR-NH2 substrate (Prod. No. BML-P132) (10µM) per minute at 37°C, in 25mM TRIS, pH 9.0.
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, screen inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Salts (sodium chloride, calcium chloride, etc.) in the assay are inhibitory. ADAM17/TACE is stable after 6 freeze-thaws at ~0.4µg/µl; freeze-thaw stability of more dilute preparations has not been tested and could lead to loss of activity.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Scientific Background: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.
Regulatory Status:RUO - Research Use Only
ADAM17 (catalytic domain) (human), (recombinant) (His-tag) SDS-PAGE
SDS-PAGE analysis: Lane 1: MW Marker; Lane 2: 1.0 µg of Prod. No. BML-SE268 ADAM17 (catalytic domain) (human), (recombinant) (His-tag).
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ADAM17 (catalytic domain) (human), (recombinant) (His-tag) SDS-PAGE

Product Literature References

Glycosylation of a disintegrin and metalloprotease 17 affects its activity and inhibition: A. Chavaroche, et al.; Anal. Biochem. 449, 68 (2014), Abstract; Full Text
Strain-induced differentiation of fetal type II epithelial cells is mediated via the integrin α6β1-ADAM17/tumor necrosis factor-α-converting enzyme (TACE) signaling pathway: Y. Wang, et al.; J. Biol. Chem. 288, 288 (2013), Abstract; Full Text
The discovery of novel tartrate-based TNF-alpha converting enzyme (TACE) inhibitors: K.E. Rosner, et al.; Bioorg. Med. Chem. Lett. 20, 1189 (2010), Abstract;
Synthesis and activity of quinolinylmethyl P1’ alpha-sulfone piperidine hydroxamate inhibitors of TACE: C. Zhang, et al.; Bioorg. Med. Chem. Lett. 19, 3445 (2009), Abstract;
TNF-alpha convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha: I.R. Patel, et al.; J. Immunol. 160, 4570 (1998), Abstract;

General Literature References

Insulin-like growth factor-1 (IGF-1)-induced processing of amyloid-{beta} precursor protein (APP) and APP-like protein 2 is mediated by different metalloproteinases: K.T. Jacobsen, et al.; J. Biol. Chem. 285, 10223 (2010), Abstract;
Novel TACE inhibitors in drug discovery: a review of patented compounds: P.R. Murumkar, et al.; Expert Opin. Ther. Pat. 20, 31 (2010), Abstract;
ADAM17 as a therapeutic target in multiple diseases: J. Arribas & C. Esselens; Curr. Pharm. Des. 15, 2319 (2009), Abstract;
Inhibition of tumor necrosis factor-alpha-converting enzyme by a selective antagonist protects brain from focal ischemic injury in rats: X. Wang, et al.; Mol. Pharmacol. 65, 890 (2004), Abstract;
Membrane-anchored CD40 is processed by the tumor necrosis factor-alpha-converting enzyme. Implications for CD40 signaling: C. Contin, et al.; J. Biol. Chem. 278, 32801 (2003), Abstract;
Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1): K.J. Garton, et al.; J. Biol. Chem. 276, 37993 (2001), Abstract;
Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha: M.L. Moss, et al.; Nature 385, 733 (1997), Abstract;

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