Recombinant Human FURIN Protein

Name: Recombinant Human FURIN Protein
Brand: Beta LifeScience
SKU: BL-078PSL
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	TG-8H-GGQ
Host Species	Human
Accession	P09958
Synonym	Furin(Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic AminoAcid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid CleavingEnzyme (Furin, Membrane Associated Receptor Protein), Proprotein ConvertaseSubtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, DibasicProcessing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin,SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleavingenzyme.
Background	Furinis a member of the peptidase S8 family. Furin signifies the ubiquitousendoprotease activity within constitutive secretory pathways aswell as capable of cleavage at the RX (K/R) R consensus motif. Furin is considered to be one of the proteases responsiblefor the activation of HIV envelope glycoproteins gp160 as well as gp140 andmight take part in tumor progression. Among the diseases associated with FURINare dementia, familial british and plague.
Description	FURIN Human Recombinant expressed in CHO cells is a single, non-glycosylatedpolypeptide chain containing 645a.a. (108-715 a.a) and having amolecular weight of 67.1 kDa. FURIN is fused to a TG-8H-GGQ tag at C-terminus and purified by proprietary chromatographictechniques.
Source	CHO cells
AA Sequence	Asp108-Glu715
Molecular Weight	67.1 kDa. The non-reduced and DTT-reduced proteins migrate at 65 - 75 and 70 - 80 kDa, respectively, by SDS-PAGE.
Purity	>90%, as determined by Coomasie stained SDS-PAGE.
Endotoxin	Less than 1.0 EU per µg of protein as determined by the LAL method.
Bioactivity	The activity of human Furin is measured with 50 µM of fluorogenic substrate, pERTKR-AMC, with a specific activity value greater than 75 pmol/ug/min.
Formulation	Liquid Solution. 0.22 µm filtered protein solution is in pH 8.0 buffer containing 10 mM TRIS, 1 mM CaCl2, 100 mM NaCl, and 50% glycerol.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Store at -20°C

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.