protein

Recombinant Human Protein Disulfide Isomerase

MBS142403

0.1 mg

235 USD

Recombinant Protein

Recombinant Human Protein Disulfide Isomerase

Disulfide Isomerase

PDI Human; Protein Disulfide Isomerase Human Recombinant; Protein Disulfide Isomerase; PDI; EC 5.3.4.1; Prolyl 4-hydroxylase subunit beta; Cellular thyroid hormone-binding protein; p55; P4HB; ERBA2L; PDIA1; PO4DB; DSI; GIT; PHDB; PO4HB; PROHB; P4Hbeta

protein disulfide-isomerase; Protein disulfide-isomerase; protein disulfide-isomerase; cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; glutathione-insulin transhydrogenase; p55; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; prolyl 4-hydroxylase subunit beta; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; protocollagen hydroxylase; thyroid hormone-binding protein p55; prolyl 4-hydroxylase, beta polypeptide; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta; p55

PDI

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

PDIA1_HUMAN

E Coli

508

The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Ala.

Greater than 95.0% as determined by a) Analysis by RP-HPLC. b) Analysis by SDS-PAGE.

The PDI protein (1mg/ml)solution was lyophilized from PBS pH-7. Sterile Filtered White lyophilized (freeze-dried) powder.

Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution Human PDI should be stored at 4 degree C between 2-7 days and for future use below -18 degree C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze-thaw cycles.

Isomerase Activity: 0.5 umol active RNase A min-1 umol PDI-1. According to the re-activation of reduced and denatured RNase A (Lyles, M. M. and Gilbert, H. F. (1991) Biochemistry 30, 613-619). Reductase Activity: 0.001 650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 96279632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (MartŽ ´nez-Galisteo, E., Padilla, C. A., Garcia-Alfonso, C., Lo ´pez-Barea, J., and Barcena, J. A. (1993) Biochimie (Paris) 75, 803809).

Solubility: It is recommended to reconstitute the lyophilized PDI in sterile 18M Omega -cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.

ENZYMES; Enzymes; Isomerase

Description: PDI Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids and having a molecular mass of 62.4 kDa. The PDI is fused to a 12 amino acid His tag (515 a.a. total) at N-terminal and purified by proprietary chromatographic techniques. Introduction: 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). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.

20070125

NP_000909.2

NM_000918.3

P07237

57,116 Da

Cellular Responses To Stress Pathway (645258); Chylomicron-mediated Lipid Transport Pathway (106157); Collagen Biosynthesis And Modifying Enzymes Pathway (645289); Collagen Formation Pathway (645288); Detoxification Of Reactive Oxygen Species Pathway (1127552); Disease Pathway (530764); Extracellular Matrix Organization Pathway (576262); Hedgehog Ligand Biogenesis Pathway (1127536); Lipid Digestion, Mobilization, And Transport Pathway (106111); Lipoprotein Metabolism Pathway (106156)

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; Endoplasmic reticulum; Oxidoreductase; Isomerase; Nuclear receptor co-regulator. Chromosomal Location of Human Ortholog: 17q25. Cellular Component: focal adhesion; endoplasmic reticulum lumen; endoplasmic reticulum; extracellular region; ER-Golgi intermediate compartment; plasma membrane; melanosome. Molecular Function: protein binding; enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; endopeptidase activity; protein disulfide isomerase activity. Biological Process: extracellular matrix organization and biogenesis; response to reactive oxygen species; 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

235 USD

0.5 mg

690

1 mg

1075