Rabbit anti-Human PDI Polyclonal Antibody | anti-PDI antibody

PDI antibody

Cat. Num. AAA9403111

• Gene Names: P4HB; DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; CLCRP1; ERBA2L; P4Hbeta
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry, Immunofluorescence
• Purity: Purified by antigen-affinity chromatography.
• Synonyms: PDI; Polyclonal Antibody; PDI antibody; anti-PDI antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Purity/Purification: Purified by antigen-affinity chromatography.
• Form/Format: Supplied in 0.1M Tris-buffered saline with 10% Glycerol (pH7.0). 0.01% Thimerosal was added as a preservative.
• Sequence Length: 508

• Applicable Applications for anti-PDI antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)
• Application Notes: Western blotting: 1:500-1:3000; Immunohistochemistry: 1:100-1:250; Immunofluorescence: 1:100-1:200
• Immunogen Type: Recombinant protein
• Immunogen Description: Recombinant protein fragment contain a sequence corresponding to a region within amino acids 23 and 197 of Human P4HB
• Target Name: PDI
• Preparation and Storage: Store at -20 degree C for long term preservation (recommended). Store at 4 degree C for short term use.

Testing Data

(Sample(30 ug of whole cell lysate)A: 293TB: A431C: H12997.5% SDS PAGEPrimary antibody diluted at 1: 500)

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded H520 xenograft, using PDI antibody at 1: 100 dilution.)

Immunofluorescence (IF)

(Immunofluorescence analysis of methanol-fixed A431, using PDI antibody at 1: 200 dilution.)

Related Product Information for anti-PDI antibody

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]

Product Categories/Family for anti-PDI antibody

Total protein Ab

NCBI and Uniprot Product Information

• NCBI GI #: 20070125
• NCBI GeneID: 5034
• NCBI Accession #: NP_000909
• NCBI GenBank Nucleotide #: NM_000918.3
• Molecular Weight: 57,116 Da
• 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; CLCRP1; ERBA2L; P4Hbeta
• NCBI Protein Information: protein disulfide-isomerase
• 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: Endoplasmic reticulum; Nuclear receptor co-regulator; Isomerase; Oxidoreductase; EC 5.3.4.1

Chromosomal Location of Human Ortholog: 17q25

Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; ER-Golgi intermediate compartment; external side of plasma membrane; extracellular region; focal adhesion; melanosome

Molecular Function: endopeptidase activity; enzyme binding; integrin binding; procollagen-proline 4-dioxygenase activity; protein binding; protein disulfide isomerase activity; protein heterodimerization activity

Biological Process: cell redox homeostasis; extracellular matrix organization and biogenesis; lipoprotein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; positive regulation of virion penetration into host cell; protein folding; proteolysis; response to reactive oxygen species

Disease: Cole-carpenter Syndrome 1