Recombinant human P4HB protein (His tag)
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Recombinant human P4HB protein (His tag) is a Human Full Length protein, in the 18 to 508 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS, Mass Spec.
View Alternative Names
ERBA2L, PDI, PDIA1, PO4DB, P4HB, Protein disulfide-isomerase, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human P4HB protein (His tag) (AB206803)
15% SDS-PAGE analysis of ab206803 : 3μg loaded
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
P4HB functions in protein folding and assembly. By acting as a chaperone it protects proteins from misfolding and aggregation. P4HB operates as part of a larger multi-protein complex that assists in maintaining protein structure under stress conditions in the cell. Its activity ensures protein stability and proper cellular function important for cell viability and health.
Pathways
P4HB plays a central role in the unfolded protein response (UPR) and oxidative protein folding pathway. It interacts with proteins such as calnexin and calreticulin through its involvement in these pathways. During oxidative protein folding P4HB introduces disulfide bonds into nascent proteins while removing incorrect ones ensuring efficient protein quality control.
Specifications
Form
Liquid
General info
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 and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed : 32149426). 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 as 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 (PubMed : 21670307).
Sequence similarities
Belongs to the protein disulfide isomerase family.
Post-translational modifications
Phosphorylation of Ser-357 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone (PubMed:32149426). It also promotes interaction with ERN1 (PubMed:32149426).
Target data
Product promise
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