A 17aa synthetic peptide near the C-terminus of rat TACE (KLH). Species Sequence Homology: Mouse - 100%, human - 94%.
Beta-amyloid (Ab) deposition in the brain is the hallmark of Alzheimers Disease (AD). To initiate Ab formation, beta-secretase cleaves APP at the N-terminus of Ab to release APPsb (~100kD soluble NT-fragment), and C99, a 12kD CT membrane fragment. Alternatively, alpha-secretase cleaves within the Ab to prevent the formation of Ab. Cleavage by alpha-secretase produces a soluble N-terminal fragment, APPsa, and a 10kD membrane C-terminal fragment, C83. Both C99 and C83 can be further cleaved by gamma-secretase releasing Ab and a nonpathogenic p3 peptide, respectively. Recently TACE, a member of the ADAM family (A Disintegrin And Metalloprotease family) protease has been shown to play a central role in a regulated cleavage of human APP. Inhibition of TACE affects both APP secretion and Ab formation in cultured cells (1). Membrane-bound TNF-a, like APP, is transmembrane protein that can undergo TACE-mediated proteolysis to release the extracellular domain as soluble TNF-a. TACE contain an autoinhibitory domain that must be removed for activity, a proteolytic domain, a disintegrin domain, a cysteine-rich domain and a transmembrane domain. Applications: Suitable for use in ELISA. Western Blot, though not tested, may potentially be used as an application. Other applications not tested. Recommended Dilution: ELISA: 1:10,000-1:100,000 using 50-100ng of control peptide/well. See cat T0500-10A. Western Blot: 1-10ug/ml using ECL. Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. 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.
Purity:
Purified by immunoaffinity chromatography.
Form:
Supplied as a liquid in PBS, pH 7.4, 0.1% BSA, 40% glycerol.
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