Mouse Monoclonal Antibody to Pdi1p Cat# MCA-38H8

      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/

      This antibody is specific for a yeast protein and so is not appropriate for IHC on mammalian material.

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).