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Gibco™ Human Furin Recombinant Protein, PeproTech®

Product Code. 17884743
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Quantity:
10 μg
10 x 50 μg
2 μg
2 x 50 μg
20 x 50 μg
5 x 50 μg
50 μg
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1mg
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500µg
50µg
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Product Code. Quantity unitSize
17884743 10 μg 10µg
17883903 2 x 50 μg 100µg
17824743 20 x 50 μg 1mg
17864663 5 x 50 μg 250µg
17874253 2 μg 2µg
17814193 10 x 50 μg 500µg
17804033 50 μg 50µg
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Product Code. 17884743 Supplier Gibco™ Supplier No. 4504710UG

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Description

Recombinant Protein

450-47-100UG will be provided as 2 x 50 μg (450-47-50UG). 450-47-1MG will be provided as 20 x 50 μg (450-47-50UG). 450-47-250UG will be provided as 5 x 50 μg (450-47-50UG). 450-47-500UG will be provided as 5 x 100 μg (450-47-50UG). Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag. This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Furin is a membrane-associated, calcium-dependent, serine protease that belongs to the subtilisin-like prohormone convertase (PC) family. Members of this family of cellular enzymes cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. Furin and other PC family members share structural similarities which include a heterogeneous ∽10 kDa amino-terminal proregion, a highly conserved ∽55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. Furin is the only known PC to possess a transmembrane domain. Cleavage of target proteins occurs at the carboxyl-terminus of the furin consensus sequence, RX(K/R)R. It has been shown that the acidic peptide sequence, C771PSDSEEDEG780, localizes furin to the trans-Golgi-network. Phosphorylation of serine residues within this region modulates intracellular routing of furin protein. An additional signaling domain includes the tetrapeptide sequence, Y759KGL762, which directs internalization from the cell surface.
TRUSTED_SUSTAINABILITY

Specifications

Accession Number P09958
For Use With (Application) Functional Assay
Formulation protein with no preservative
Gene ID (Entrez) 5045
Molecular Weight (g/mol) 63.9 kDa
Name Human Furin
Quantity 10 μg
Source Insect cells
Regulatory Status RUO
Endotoxin Concentration <1 EU/ μg
Gene Alias 9130404I01Rik; dibasic processing enzyme; dibasic-processing enzyme; FES upstream region; FUR; Furin; furin (paired basic amino acid cleaving enzyme); furin, membrane associated receptor protein; furin, paired basic amino acid cleaving enzyme; furin; LOW QUALITY PROTEIN: furin; Pace; Paired basic amino acid cleaving enzyme (furin); paired basic amino acid residue cleaving enzyme; paired basic amino acid residue-cleaving enzyme; Pcsk3; prohormone convertase 3; proprotein convertase subtilisin/kexin type 3; Proprotein convertase subtilisin/kexin type 3 (paired basic amino acid cleaving enzyme, furin, membrane associated receptor protein); proprotein convertase subtilisin/kexin type3; SPC1; subtilisin pro-protein processing enzyme
Common Name Furin
Gene Symbol FURIN
Biological Activity Measured by its ability to cleave the fluorogenic peptide substrate Boc-Arg-Val-Arg-Arg-AMC (Bachem Catalog# I-1645.0025).
Conjugate Unconjugated
Recombinant Recombinant
Protein Tag His-tag
Sequence 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 CAPCHACSAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEHHHHH HHH
Content And Storage -20°C
Expression System Insect cells
Form Lyophilized
Purity or Quality Grade ≥ 95% by SDS-PAGE gel and HPLC analyses.
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