Rabbit PDI Polyclonal Antibody | anti-Pdia2 antibody

PDI Antibody: Biotin

Cat. Num. AAA805163

• Gene Names: Pdia2; Pdip
• Reactivity: Human, Mouse, Rat, Dog, Hamster, Monkey, Guinea Pig, Bovine, Sheep, Pig, Xenopus
• Applications: Western Blot, Immunoprecipitation, Immunocytochemistry, Immunohistochemistry
• Synonyms: PDI; Polyclonal Antibody; PDI Antibody: Biotin; PDA2; PDIA2; PDIP; pancreatic protein disulfide isomerase; anti-Pdia2 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat, Dog, Hamster, Monkey, Guinea Pig, Bovine, Sheep, Pig, Xenopus
• Clonality: Polyclonal
• Form/Format: Rabbit Antiserum
• Sequence Length: 527

• Applicable Applications for anti-Pdia2 antibody: Western Blot (WB), Immunoprecipitation (IP), Immunocytochemistry (ICC), Immunohistochemistry (IHC)
• Application Notes: 1:4000 (WB)
• Conjugate: Biotin
• Storage Buffer: Rabbit antiserum
• Preparation and Storage: -20 degree C

Western Blot (WB)

(Western blot analysis of Rat tissue mix showing detection of PDI protein using Rabbit Anti-PDI Polyclonal Antibody (SPC-114). Load: 15 ugprotein. Block: 1.5% BSA. Primary Antibody: Rabbit Anti-PDI Polyclonal Antibody (SPC-114) at 1:4000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.)

Related Product Information for anti-Pdia2 antibody

Background Info: Detects ~58kDa

Scientific Background: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation via its oxidase activity and isomerization via its isomerase activity, as well as the reduction of disulphide bonds in proteins (1). Studies suggest BiP and PDI work together sequentially to increase oxidation of these proteins (2, 3). PDI has also been found to function as a chaperone to prevent the aggregation of unfolded substrates, and serves as a subunit of prolyl 4-hydroxylase and microsomal triglyceride transferase (4, 5). PDI is an abundant 55kDa protein located primarily in the ER, however studies have also proved its presence in the cytosol (1). PDI has the ability to reside in the ER permanently due to the highly conserved KDEL sequence at its carboxy-terminus (6). It uses carboxy-terminal KDEL as a retention signal, and this appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor (7).

Product Categories/Family for anti-Pdia2 antibody

Chaperones; Organelle Markers

References

1. NA K.S. et al. (2007) Mol Cells. 24(2): 261-7. 2. Mayer M., Kies U., Kammermeier R., and Buchner J. (2000) J Biol Chem. 275(38): 29421-5. 3. Delom F., Mallet B., Carayon P., and Lejeune P.J. (2001) J Biol Chem 276(24): 21337-42. 4. Schultz-Norton J.R., McDonald W.H., Yates J.R. and Nardulli A.M. (2006) Mol Endocrinol 20(9): 1982-95 5. Turano C., Coppari S. Altieri F. and Ferraro (2002) J Cell Physiol 193: 154-163. 6. Janiszewski M. (2005) J. Biol Chem. 280(49): 40813- 40819. 7. Yoshimori T., et al. (1990) J Biol Chem. 265(26): 15984-90.

NCBI and Uniprot Product Information

• NCBI GI #: 164663906
• NCBI GeneID: 287164
• NCBI Accession #: NP_001099245.2
• NCBI GenBank Nucleotide #: NM_001105775.2
• UniProt Accession #: P04785; P13700
• Molecular Weight: 56,951 Da
• NCBI Official Full Name: protein disulfide-isomerase A2
• NCBI Official Synonym Full Names: protein disulfide isomerase family A, member 2
• NCBI Official Symbol: Pdia2
• NCBI Official Synonym Symbols: Pdip
• NCBI Protein Information: protein disulfide-isomerase A2; protein disulfide isomerase A2; protein disulfide isomerase, pancreatic; protein disulfide isomerase associated 2
• UniProt Protein Name: Protein disulfide-isomerase
• Protein Family: Protein disulfide-isomerase
• UniProt Gene Name: P4hb
• UniProt Synonym Gene Names: Pdia1; PDI
• UniProt Entry Name: PDIA1_RAT

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

Cellular Component: focal adhesion; endoplasmic reticulum lumen; endoplasmic reticulum; melanosome; plasma membrane; ER-Golgi intermediate compartment

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

Biological Process: protein folding; cell redox homeostasis; peptidyl-proline hydroxylation to 4-hydroxy-L-proline