SCP0148
Furin Inhibitor II Peptide
≥95% (HPLC), lyophilized powder
Synonym(s):
Hexa-D-arginine amide
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About This Item
Empirical Formula (Hill Notation):
C36H75N25O6
Molecular Weight:
954.14
UNSPSC Code:
12352202
NACRES:
NA.32
Recommended Products
product name
Furin Inhibitor II,
Assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥48%
storage condition
protect from light
technique(s)
protein extraction: suitable
storage temp.
−20°C
Amino Acid Sequence
Mpa-Mpa-Mpa-Mpa-Mpa-Mpa
General description
Furin is a calcium-dependent serine endoproteinase and belongs to the subtilisin-like proprotein/prohormone convertase (PC) family. It is distributed ubiquitously and has a rhythmic movement between the trans-Golgi network, cell surface and the endosomes.
Application
Furin Inhibitor II has been used as a furin inhibitor:
- to study its effects on transforming growth factor β1 (TGF-β1) induced glial cell line-derived neurotrophic factor (GDNF) production in non-tumorigenic immortalized human granulosa cell line (SVOG).
- to study its effect on cleavage of (Pro) renin receptor (PRR) induced by bovine serum albumin (BSA) in human kidney 2 (HK-2) cells.
- in furin cleavage assay.
Biochem/physiol Actions
Furin plays a role in processing several pro-proteins such as, bone morphogenetic protein 4 (BMP-4), insulin receptor and Notch1 receptor. It also processes human immune deficiency virus 1 (HIV-1) glycoprotein gp160, several metalloproteases and pro-β-nerve growth (pro-β-NGF) factor. Furin is also involved in cleaving transforming growth factor β1 (TGF-β1).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme
Dubois C M, et al.
The American Journal of Pathology, 158(1), 305-316 (2001)
A Cameron et al.
The Journal of biological chemistry, 275(47), 36741-36749 (2000-08-26)
The ubiquitous serine endoprotease furin has been implicated in the activation of bacterial toxins and viral glycoproteins as well as in the metastatic progression of certain tumors. Although high molecular mass bioengineered serpin inhibitors have been well characterized, no small
Marcel Westenberg et al.
Journal of virology, 76(1), 178-184 (2001-12-12)
The Spodoptera exigua multicapsid nucleopolyhedrovirus (SeMNPV) Se8 gene was recently shown to encode the viral envelope fusion (F) protein. A 60-kDa C-terminal subunit (F1) of the 76-kDa primary translation product of this gene was found to be the major envelope
Miroslav S Sarac et al.
Infection and immunity, 70(12), 7136-7139 (2002-11-20)
The Pseudomonas aeruginosa exotoxin A (PEA) protein requires furin-mediated cleavage for manifestation of toxicity. We show here that the small stable furin inhibitor hexa-D-arginine amide effectively blocks PEA-induced cell lysis and is itself noncytotoxic. Administration of hexa-D-arginine to PEA-treated mice
Miroslav S Sarac et al.
Infection and immunity, 72(1), 602-605 (2003-12-23)
The anthrax toxin protective antigen precursor is activated by proteolytic cleavage by furin or a furin-like protease. We present here data demonstrating that the small stable furin inhibitor hexa-D-arginine amide delays anthrax toxin-induced toxemia both in cells and in live
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