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PDIA1 Antibody [Knockout Validated]

Purified Mouse Monoclonal Antibody (Mab)

     
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  • 1 - PDIA1 Antibody [Knockout Validated] AM8515b
    All lanes : Anti-PDIA1 Antibody at 1:1000 dilution (upper) Lane 1: HeLa Lane 2: HeLa-Knockout Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Mouse IgG, (H+L), Peroxidase conjugated (ASP1613) at 1/8000 dilution. Predicted band size : 57 kDa
  • 1 - PDIA1 Antibody [Knockout Validated] AM8515b
    All lanes : Anti-PDIA1 Antibody at 1:4000 dilution Lane 1: Hela whole cell lysate Lane 2: MCF-7 whole cell lysate Lane 3: HepG2 whole cell lysate Lane 4: PANC-1 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 57 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P07237
Reactivity Human
Host Mouse
Clonality monoclonal
Isotype IgG1,k
Clone Names 1530CT836.11.53
Calculated MW 57116 Da
Additional Information
Gene ID 5034
Other Names Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55, P4HB, ERBA2L, PDI, PDIA1, PO4DB
Target/Specificity This PDIA1 antibody is generated from a mouse immunized with a recombinant protein of human PDIA1.
Dilution WB~~1:4000
E~~Use at an assay dependent concentration.
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsPDIA1 Antibody [Knockout Validated] is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name P4HB
Synonyms ERBA2L, PDI, PDIA1, PO4DB
Function 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 and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). 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 as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
Cellular Location Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces (PubMed:11181151). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:10636893) Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612) {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:11181151, ECO:0000269|PubMed:23475612, ECO:0000305}
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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.

REFERENCES

Pihlajaniemi T.,et al.EMBO J. 6:643-649(1987).
Cheng S.-Y.,et al.J. Biol. Chem. 262:11221-11227(1987).
Tasanen K.,et al.J. Biol. Chem. 263:16218-16224(1988).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.

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