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Furin convertase substrate (fluorogenic)

 
ALX-260-040-M001 1 mg 65.00 USD
 
ALX-260-040-M005 5 mg 145.00 USD
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Replaces Prod. #: BML-P143

Fluorogenic substrate for furin/SPC1/PACE/PCSK3 and other subtilisin/kexin-like proprotein convertases such as Kex2, SPC2/PC2/PCSK2, SPC3/PCSK1, PACE4/SPC4/PCSK6, SPC5/PC4/PCSK4, SPC6/PC5/PC6/PCSK5, and SPC7/LPC/PC7/PC8/PCSK7. Can be used on live cells. Ex: 360-380 nm, Em: 440-460 nm.

Product Details

Alternative Name:Boc-RVRR-AMC, Boc-Arg-Val-Arg-Arg-AMC
 
Sequence:Boc-Arg-Val-Arg-Arg-AMC (AMC=7-Amino-4-methylcoumarin)
 
Formula:C38H62N14O8
 
MW:843.0
 
CAS:136132-77-9
 
Purity:≥95% (HPLC; TLC)
 
Appearance:White to off-white powder.
 
Solubility:Soluble in water (10mg/ml) or DMSO.
 
Shipping:Ambient Temperature
 
Long Term Storage:-20°C
 
Handling:Protect from light.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

The Proprotein Convertase Furin Contributes to Rhabdomyosarcoma Malignancy by Promoting Vascularization, Migration and Invasion: P. Jaaks, et al.; PLoS One 11, e0161396 (2016), Abstract; Full Text
Cleavage of the HPV16 Minor Capsid Protein L2 during Virion Morphogenesis Ablates the Requirement for Cellular Furin during De Novo Infection: L. Cruz, et al.; Viruses 7, 5813 (2015), Application(s): In vitro Furin enzyme-treatment of fluorogenic furin assay, Abstract; Full Text
Fluid shear stress promotes proprotein convertase-dependent activation of MT1-MMP: H. Kang, et al.; Biochem. Biophys. Res. Commun. 460, 596 (2015), Application(s): Fluorescence Microscopy, Abstract;
A proprotein convertase/MMP-14 proteolytic cascade releases a novel 40?kDa vasculostatin from tumor suppressor BAI1: S.M. Cork, et al.; Oncogene 31, 5144 (2012), Abstract; Full Text
Production, purification, and characterization of recombinant prohormone convertase 5 from baculovirus-infected insect cells: B.M. Cain, et al.; Protein Expr. Purif. 24, 227 (2002), Abstract;
Molecular cloning of kpcA gene encoding a Kex2p-like endoprotease from Aspergillus nidulans: B.K. Kwon, et al.; Mol. Cells 12, 142 (2001), Abstract;
Enzymic characterization in vitro of recombinant proprotein convertase PC4: A. Basak, et al.; Biochem. J. 343, 29 (1999), Abstract;
Quantitative characterization of furin specificity. Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamides: D.J. Krysan, et al.; J. Biol. Chem. 274, 23229 (1999), Abstract;
In vitro characterization of the novel proprotein convertase PC7: J.S. Munzer, et al.; J. Biol. Chem. 272, 19672 (1997), Abstract;
PACE4: a subtilisin-like endoprotease with unique properties: R.E. Mains, et al.; Biochem. J. 321, 587 (1997), Abstract;
Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules: A.V. Azaryan, et al.; J. Biol. Chem. 270, 8201 (1995), Abstract;
Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen: S.S. Molloy, et al.; J. Biol. Chem. 267, 16396 (1992), Abstract; Full Text
Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells: K. Hatsuzawa, et al.; J. Biol. Chem. 267, 16094 (1992), Abstract; Full Text

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