P4HB, Recombinant Protein

Prolyl 4-hydroxylase subunit beta; P4Hbeta; PDI; PDIA1; PHD; PO4DB; PO4HB; ERBA2L; Prolyl 4-hydroxylase subunit beta

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 90% by SDS-PAGE

Liquid. In 20 mM Tris-HCl (pH 8.0) containing 10% glycerol

1 mg/ml (determined by Bradford assay) (lot specific)

Can be stored at 4 degree C short term (1-2 weeks).
For long term storage, aliquot and store at -20 degree C or -70 degree C.
Avoid repeated freezing and thawing cycles.

Small volumes of P4HB recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

P4HB, prolyl 4 hydroxylase subunit beta, is a multifunctional and highly abundant enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This protein is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Recombinant human P4HB protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography.

Heat Shock Proteins

SDS-PAGE

57.5 kDa (512aa), confirmed by MALDI-TOF

prolyl 4-hydroxylase subunit beta

protein disulfide-isomerase

Protein disulfide-isomerase

ERBA2L; PDI; PDIA1; PO4DB; PDI  [Similar Products]

This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. [provided by RefSeq, Jul 2008]

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 (PubMed:21670307).

Pfander D., et al. (2006) Am J Pathol. 169 (2):491-502.; Kivirikko KI., (1991) J Hepatol. 13 Suppl 3:S2-7.;

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