FURIN Human

Furin Human Recombinant
Cat. No.
BT10685
Source
Escherichia Coli.
Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa.
FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Furin, a member of the peptidase S8 family, is a ubiquitous endoprotease found within constitutive secretory pathways. It is known for its ability to cleave at the RX(K/R)R consensus motif. Furin plays a crucial role in activating HIV envelope glycoproteins gp160 and gp140 and may contribute to tumor progression. Several diseases, including dementia, familial British, and plague, are associated with FURIN.
Description
Recombinant human FURIN, produced in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 69.8 kDa. It consists of 645 amino acids, spanning from residues 108 to 715. The protein includes a 37 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The FURIN protein solution is provided at a concentration of 1 mg/ml and contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for extended storage. Avoid repeated freezing and thawing cycles.
Purity
The purity is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

Product Science Overview

Introduction

Furin is a membrane-associated, calcium-dependent serine protease that belongs to the subtilisin-like proprotein convertase (PC) family . This enzyme plays a crucial role in the proteolytic maturation of a wide variety of precursor proteins, including hormones, growth factors, receptors, and enzymes . Recombinant human furin is produced using various expression systems to study its function and potential therapeutic applications.

Structure and Function

Furin is synthesized as an inactive zymogen and undergoes autocatalytic cleavage to become active . The active enzyme is composed of several domains, including a propeptide domain, a catalytic domain, a P-domain, and a transmembrane domain . The catalytic domain is responsible for the enzyme’s proteolytic activity, while the P-domain is involved in substrate recognition and binding .

Furin cleaves its substrates at specific sites, typically characterized by the sequence R-X-K/R-R, where X can be any amino acid . This cleavage is essential for the activation of many proproteins, including prohormones, neuropeptide precursors, viral proteins, and bacterial toxins .

Biological Significance

Furin is ubiquitously expressed in various tissues and is involved in numerous physiological processes . In the brain, furin processes proproteins of growth factors, receptors, and enzymes, playing a vital role in neuronal survival, axon growth, dendritic development, synaptogenesis, and neurodegeneration . Aberrant activity of furin has been associated with a wide range of pathological events, including cancer, cardiovascular disorders, infectious diseases, and neurological diseases .

Recombinant Production

Recombinant human furin is produced using various expression systems, including mammalian cells, insect cells, and bacteria . The recombinant protein is typically purified to high purity and validated for its proteolytic activity . For example, recombinant human furin expressed in vaccinia virus-infected BSC-40 cells has been shown to have high proteolytic activity and purity .

Applications

Recombinant human furin is widely used in research to study its role in various biological processes and diseases . It is also used in the development of therapeutic interventions targeting furin activity. For instance, furin inhibitors are being explored as potential treatments for diseases where furin activity is dysregulated, such as cancer and viral infections .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.