Recombinant Human Protein disulfide-isomerase protein (P4HB), partial (Active)

SKU:BHP10500251
Featured Peer-Reviewed Research Validated
Overview
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Recombinant P4HB Human protein produced in E. coli, N-terminal 6xHis-tagged spanning 19-508aa. Suitable for binding assays, functional studies, and assay development.
Expression System E. coli
Tag N-terminal 6xHis-tagged
Purity >95%
Species Human
Molecular Weight 56.6 kDa
Biological Activity Validated
Options selector
Catalog no. Size
CSB-AP000091HU-500UG 500 ug
CSB-AP000091HU-100UG 100 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (2) - 500 ug, 100 ug
  • Lead time: In Stock at Manufacturer. Lead time is typically 5-10 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No CSB-AP000091HU
Activity
  • Yes
Alternative Names PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55,
Biological Activity Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity increase at 650 nm due to insulin reduction.The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time.
Endotoxin Level Less than 1.0 EU/μg as determined by LAL method.
Expression System
  • E. coli
Form Lyophilized powder
Function
  • This multifunctional protein catalyzes the formation
  • breakage and rearrangement of disulfide bonds. At the cell surface
  • seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell
  • seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations
  • functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations
  • facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells
  • increasing disulfide reductase activity at the plasma membrane
  • altering the plasma membrane redox state and enhancing cell migration
Molecular Weight 56.6 kDa
Product Type
  • Recombinant Protein
Purity >95% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # P07237

Scientific Background

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins.

Product Description

E. coli Expression

Recombinant Human Protein disulfide-isomerase protein (P4HB), partial (Active) is a recombinant protein expressed in E. coli and purified to >95% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Lyophilized powder, n-terminal 6xhis-tagged. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 56.6 kDa
Expression Region 19-508aa
Expression System E. coli
Tag N-terminal 6xHis-tagged
Purity >95% as determined by SDS-PAGE.
Form Lyophilized powder
Storage Buffer Lyophilized from a 0.2 µm filtered PBS, pH 7.0
Endotoxin Level Less than 1.0 EU/μg as determined by LAL method.
UniProt Accession P07237
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Functional Activity

Biologically Validated

Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity increase at 650 nm due to insulin reduction.The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as N-terminal 6xHis-tagged and has been purified to >95% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Yes. Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity increase at 650 nm due to insulin reduction.The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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