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Boc-Gln-Ala-Arg-AMC

Protease substrate
 
BML-P237-0005 5 mg 115.00 USD
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Sold as net peptide weight.
Fluorogenic substrate for trypsin (kcat/Km=2.0 x 107 M-1sec-1; Km=6.0 µM); matriptase/MT-SP1 and matriptase-2/TMPRSS6; PRSS12; KLK5; KLK11/PRSS20, KLK12, and KLK14; tryptase and thrombin; and dust mite allergen Der p 1. Ex.: 380 nm, Em.: 460 nm, although the following Ex/Em can also be used: 355,375/440,450. This substrate is useful for inhibitor screening and kinetic analysis. Also available: fluorogenic calibration standard AMC (BML-KI144).

Product Specification

Alternative Name:Boc-QAR-AMC
 
Sequence:N-tert-butoxycarbonyl-Gln-Ala-Arg-AMC  [AMC=7-amino-4-methylcoumarin]
 
Formula:C29H42N8O8
 
MW:630.7
 
Purity:≥99% (HPLC)
 
Appearance:Lyophilized solid.
 
Solubility:Soluble in DMSO (≥10mM) or methanol (50mg/ml).
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Use/Stability:Protect from light and moisture.
 

Product Literature References

Human cancer cells retain modest levels of enzymatically active matriptase only in extracellular milieu following induction of zymogen activation: L.L. Chu, et al.; PLoS One 9, e92244 (2014), Application(s): Use of Boc-QAR-AMC to measure matriptase activity, Abstract; Full Text
Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes: Y.W. Chen, et al.; PLoS One 8, e62826 (2013), Application(s): Use of Boc-QAR-AMC to measure matriptase activity, Abstract; Full Text
Matriptase is a novel initiator of cartilage matrix degradation in osteoarthritis: J.M. Milner, et al.; Arthritis Rheum. 62, 1955 (2010), Application(s): Use of Boc-QAR-AMC to measure matriptase activity, Abstract; Full Text
Enzymatic properties and localization of motopsin (PRSS12), a protease whose absence causes mental retardation: S. Mitsui, et al.; Brain Res. 1136, 1 (2007), Abstract;
Enzymatic properties of human kallikrein-related peptidase 12 (KLK12): N. Memari, et al.; Biol. Chem. 388, 427 (2007), Abstract;
Expression and enzymatic characterization of recombinant human kallikrein 14: S. Rajapakse, et al.; Zoolog. Sci. 24, 774 (2007), Abstract;
Biochemical and enzymatic characterization of human kallikrein 5 (hK5), a novel serine protease potentially involved in cancer progression: I.P. Michael, et al.; J. Biol. Chem. 280, 14628 (2005), Abstract;
Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins: G. Velasco, et al.; J. Biol. Chem. 277, 37637 (2002), Abstract;
Synthesis and physical characterization of a P1 arginine combinatorial library, and its application to the determination of the substrate specificity of serine peptidases: S. T. Furlong, et al.; Bioorg. Med. Chem. 10, 3637 (2002), Abstract;
A novel isoform of a kallikrein-like protease, TLSP/hippostasin, (PRSS20), is expressed in the human brain and prostate: S. Mitsui, et al.; BBRC 272, 205 (2000), Abstract;
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease: S. L. Lee, et al.; J. Biol. Chem. 275, 36720 (2000), Abstract;
A sensitive fluorescent assay for measuring the cysteine protease activity of Der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus: O. Schulz, et al.; Mol. Pathol. 51, 222 (1998), Abstract;
Isolation and characterization of a novel serine proteinase complexed with alpha 2-macroglobulin from porcine gastric mucosa: T. Uchino, et al.; J. Biol. Chem. 268, 527 (1993), Abstract;
Highly sensitive peptide-4-methylcoumaryl-7-amide substrates for blood-clotting proteases and trypsin: S. Kawabata, et al.; Eur. J. Biochem. 172, 17 (1988), Abstract;

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