| Name: | Mouse Monoclonal to Anti-Pdi1p, protein disulfide isomerase |
| Immunogen: | Yeast nuclear preparations |
| HGNC Name: | NA |
| UniProt: | P17967 |
| Molecular Weight: | 58.2kDa |
| Host: | Mouse |
| Isotype: | IgG1 |
| Species Cross-Reactivity: | Saccharomyces cerevisiae |
| RRID: | AB_2156463 |
| Format: | Concentrated hybridoma cell culture media plus 5mM NaN3 |
| Applications: | WB, IF, IP |
| Recommended Dilutions: | WB: 1:10,000. IF: 1:500-1:1,000 |
| Storage: | Store at 4°C for short term, for longer term at -20°C. Avoid freeze/thaw cycles. |
Western blots of whole yeast protein extracts with a collection of EnCor antibodies directed against yeast proteins. The blot for MCA-38H8 is in the indicated lane, 6th from the left, and the number indicates the SDS-PAGE molecular weight in kiloDaltons.
Mouse Monoclonal Antibody to Pdi1p
Cat# MCA-38H8
$120.00 – $800.00
Pdi1p is a yeast protein disulfide isomerase. It is a major endoplasmic reticulum protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins. It also has a role in recognizing proteins targeted for ER-associated degradation (ERAD) and is a member of the protein disulfide isomerase family. Proteins in this family also can break disulfide bonds on substrate proteins. The protein is also known as Eps1p.
The MCA-38H8 antibody was generated by immunizing a mouse with a preparation of yeast nuclei followed by monoclonal antibody production. Western blots of yeast protein extracts probed with the MCA-38H8 antibody revealed a ~65kDa band, and immunofluorescence staining gave an endoplasmic reticulum staining pattern. The specificity of the antibody was determined by screening a yeast genomic expression library in phage λ-gt11. Four different clones from the library all contain different overlapping regions of Pdi1p. The Pdi1p protein is expressed in the endoplasmic reticulum and nuclear envelope of yeast cells.
Pdi1p is a yeast protein disulfide isomerase. It is a major endoplasmic reticulum protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins. It also has a role in recognizing proteins targeted for ER-associated degradation (ERAD) and is a member of the protein disulfide isomerase family. Proteins in this family also can break disulfide bonds on substrate proteins. The protein is also known as Eps1p.
Western blots of yeast protein extracts probed with 38H8 diluted 1/20,000 (ECL detection) reveal a ~65 kDa band (Initial dilution range: 1/5,000 – 1/10,000). Immunofluorescence using yeast cells with MCA-38H8 gives an endoplasmic reticulum staining pattern, and for this purpose should be used at a dilution of 1/500 to 1/5,000. The specificity of the mAb was determined by screening a yeast genomic library in phage lgt11. Four different clones from the library all contain different overlapping regions of Pdi1p. Pdi1p has a predicted protein size of 58.2 kDa. The subcellular localization of the the protein is the endoplasmic reticulum and nuclear envelope. Antibody is provided as 500 µL of sterile-filtered cell culture fluid from an Integra CL-350 biochamber plus sodium azide. The isotype is IgG1 with a light k chain.
Saccharomyces Genome Database (SGD) Link: Press here
1. Elrod-Erickson MJ1, Kaiser CA. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell 7:1043-58 (1996).
