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Anti-ERp57 Picoband Antibody
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- BACKGROUND
Application 
| WB, IHC-P, IHC-F |
|---|---|
| Primary Accession | P30101 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Protein disulfide-isomerase A3(PDIA3) detection. Tested with WB, IHC-P, IHC-F in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 2923 |
|---|---|
| Other Names | Protein disulfide-isomerase A3, 5.3.4.1, 58 kDa glucose-regulated protein, 58 kDa microsomal protein, p58, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 57, ER protein 57, ERp57, Endoplasmic reticulum resident protein 60, ER protein 60, ERp60, PDIA3, ERP57, ERP60, GRP58 |
| Calculated MW | 56782 MW KDa |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, By Heat Immunohistochemistry(Frozen Section), 0.5-1 µg/ml Western blot, 0.1-0.5 µg/ml |
| Subcellular Localization | Endoplasmic reticulum. Endoplasmic reticulum lumen . Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
| Tissue Specificity | Detected in the flagellum and head region of spermatozoa (at protein level). . |
| Protein Name | Protein disulfide-isomerase A3 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human ERp57 (471-505aa RELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL), different from the related mouse and rat sequences by two amino acids. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Name | PDIA3 (HGNC:4606) |
|---|---|
| Synonyms | ERP57, ERP60, GRP58 |
| Function | Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323). |
| Cellular Location | Endoplasmic reticulum. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11598}. Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545). |
| Tissue Location | Detected in the flagellum and head region of spermatozoa (at protein level) (PubMed:20400973). Expressed in liver, stomach and colon (at protein level). Expressed in gastric parietal cells and chief cells (at protein level) (PubMed:24188822) |
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Provided below are standard protocols that you may find useful for product applications.
Background
PDIA3 (Protein disulfide isomerase family A, member 3), also called GRP58, Erp57 or ER60, is an isomerase enzyme. It is mapped on 15q15.3. PDIA3 is also part of the major histocompatibility complex (MHC) class I peptide-loading complex, which is essential for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface. This gene encodes a protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. The protein was once thought to be a phospholipase; however, it has been demonstrated that the protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
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