Furin convertase substrate (fluorogenic)
[Boc-RVRR-AMC, Boc RVRR AMC]
| ALX-260-040-M001 | 1 mg | 25.00 USD |  |
|
| ALX-260-040-M005 | 5 mg | 90.00 USD | |
|
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: 350 nm, Em: 460 nm, although the following Ex/Em can also be used: 330-380/440-490.
Product Specification
| Formula: | C38H62N14O8 |
| MW: | 843.0 |
| Purity: | ≥95% (HPLC) |
| Appearance: | White to off-white powder. |
| Sequence: | Boc-Arg-Val-Arg-Arg-AMC (AMC=7-Amino-4-methylcoumarin) |
| CAS: | 136132-77-9 |
| Solubility: | Soluble in water (10mg/ml) or DMSO. |
| Shipping: | AMBIENT |
| Long Term Storage: | -20°C |
| Handling: | Protect from light. |
Product Literature References
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
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;
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 (Pt 3), 587 (1997), Abstract;
Enzymic characterization in vitro of recombinant proprotein convertase PC4: A. Basak, et al.; Biochem J. 343 (Pt 1), 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;
Molecular cloning of kpcA gene encoding a Kex2p-like endoprotease from Aspergillus nidulans: B.K. Kwon, et al.; Mol. Cells 12, 142 (2001), Abstract;
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;
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