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PDIA1 Antibody
Purified Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P07237 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | monoclonal |
| Isotype | IgG1,k |
| Clone/Animal Names | 1530CT836.11.53 |
| Calculated MW | 57116 Da |
| 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 |
| 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. |
| Storage | Maintain 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. |
| Precautions | PDIA1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| 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} |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
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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