Protein Disulfide Isomerase (PDI) Recombinant Protein | PDI recombinant protein

Recombinant Protein Disulfide Isomerase (PDI)

Cat. Num. AAA2011014

• Gene Names: P4HB; DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; ERBA2L; P4Hbeta
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Protein Disulfide Isomerase (PDI); Recombinant Protein Disulfide Isomerase (PDI); PDI recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with two N-terminal Tags, His-tag and GST-tag, its sequence is listed below.; MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD GSTSGSGHHH HHHSAGLVPR GSTAIGMKET AAAKFERQHM DSPDLGTLEV LFQGPLGSEF- FEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDG
• Sequence Length: 508

• Applicable Applications for PDI recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Homo sapiens (Human)
• Expression System: Prokaryotic expression
• Residues: Phe216~Gly465 (Accession # P07237) with two N-terminal Tags, His-tag and GST-tag
• Subcellular Location: Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Predicted Isoelectric Point: 5.6
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

Sequence Information

SDS-Page

NCBI and Uniprot Product Information

• NCBI GI #: 20070125
• NCBI GeneID: 5034
• NCBI Accession #: NP_000909.2
• NCBI GenBank Nucleotide #: NM_000918.3
• UniProt Accession #: P07237; P30037; P32079; Q15205; Q6LDE5; B2RDQ2
• Molecular Weight: 60.8kDa
• NCBI Official Full Name: protein disulfide-isomerase
• NCBI Official Synonym Full Names: prolyl 4-hydroxylase, beta polypeptide
• NCBI Official Symbol: P4HB
• NCBI Official Synonym Symbols: DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; ERBA2L; P4Hbeta
• NCBI Protein Information: protein disulfide-isomerase; p55; protocollagen hydroxylase; prolyl 4-hydroxylase subunit beta; collagen prolyl 4-hydroxylase beta; thyroid hormone-binding protein p55; glutathione-insulin transhydrogenase; cellular thyroid hormone-binding protein; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; protein disulfide isomerase family A, member 1; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
• UniProt Protein Name: Protein disulfide-isomerase
• UniProt Gene Name: P4HB
• UniProt Synonym Gene Names: ERBA2L; PDI; PDIA1; PO4DB; PDI
• UniProt Entry Name: PDIA1_HUMAN

NCBI Description

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]

Uniprot Description

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: Nuclear receptor co-regulator; EC 5.3.4.1; Endoplasmic reticulum; Isomerase; Oxidoreductase

Chromosomal Location of Human Ortholog: 17q25

Cellular Component: focal adhesion; endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; extracellular region; 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: 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