protein

Protein Disulfide Isomerase (PDI), human recombinant

MBS844696

0.1 mg

245 USD

Recombinant Protein

Protein Disulfide Isomerase (PDI), human recombinant

[Protein Disulfide Isomerase (PDI)]

[Protein Disulfide Isomerase; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55]

[protein disulfide-isomerase; Protein disulfide-isomerase; protein disulfide-isomerase; prolyl 4-hydroxylase, beta polypeptide; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55]

[PDIA1]

[P4HB; P4HB; DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; CLCRP1; ERBA2L; P4Hbeta; ERBA2L; PDI; PDIA1; PO4DB; PDI]

PDIA1_HUMAN

508

>95% by SDS-PAGE and HPLC. Endotoxin level <0.1 ng per ug

Lyophilized powder

The lyophilized protein is best-stored desiccated below 0° C. Reconstituted PDI should be stored in working aliquots at -20°C. For long-term storage, it is recommended to add carrier protein (0.1% HAS or BSA).

Source: E.coli. Reconsitution: Centrifuge the vial prior to opening. Reconstitute in 50 mM Tris Buffer, pH 8.0 to a concentration of 0.1 -1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at 4°C for 1 week or –20°C for future use. Biological activity: Recombinant PDI is biological active. Reductase activity is 1.0 x 10-3?650 nm/ min-2, 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.Isomerase activity is 0.5 u mol active RNase A min-1 ?mol PDI-1, according to the re-activation of reduced and denatured RNase A.

Background: Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human PDI produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 508 amino acids and having a molecular mass of 57.1 kDa. The human PDI contains N-terminal 6xHis-tag and is purified by proprietary chromatographic techniques.

20070125

NP_000909.2

NM_000918.3

P07237

57.1 kDa

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]

PDIA1: 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. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family. Protein type: EC 5.3.4.1; Isomerase; Oxidoreductase; Endoplasmic reticulum; Nuclear receptor co-regulator. Chromosomal Location of Human Ortholog: 17q25. Cellular Component: focal adhesion; endoplasmic reticulum lumen; endoplasmic reticulum; ER-Golgi intermediate compartment; melanosome; plasma membrane; extracellular region. Molecular Function: protein binding; enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; endopeptidase activity; protein disulfide isomerase activity. Biological Process: response to reactive oxygen species; extracellular matrix organization and biogenesis; protein folding; cell redox homeostasis; lipoprotein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; proteolysis. Disease: Cole-carpenter Syndrome 1

0.1 mg

245 USD

1 mg

1170

5 mg

4090