Abcam, ab4644, Anti-PDI1 antibody [38H8]

Size: 250µL
Mouse Monoclonal PDI antibody. Suitable for WB, ICC/IF and reacts with Saccharomyces cerevisiae samples. Cited in 8 publications.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:38H8,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:No,
Reacts with:Saccharomyces cerevisiae,
Applications:WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Properties and Storage Information:
Form-Liquid, Storage buffer-Preservative: 0.065% Sodium azideConstituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Protein Disulfide Isomerase 1 (PDI1) also known as PDIA1 is a multifunctional enzyme that facilitates protein folding and thiol-disulfide exchange reactions within the endoplasmic reticulum (ER). It has a molecular weight of approximately 57 kDa. PDI1 is expressed abundantly in the endoplasmic reticulum of various cell types especially in tissues like the liver where it aids in processing secretory and membrane proteins. The protein's thioredoxin-like domains play an important role in oxidizing or reducing disulfide bonds ensuring proper protein conformation.
Biological function summary
PDI1 acts beyond conventional disulfide bond formation and isomerization. It serves as a chaperone that prevents protein aggregation during oxidative protein folding. PDI1 is part of the protein disulfide isomerase family which interacts in a complex network to maintain protein homeostasis. It works together with ERp57 and other members to assist in the quality control of nascent proteins ensuring functional and correctly folded proteins are distributed within the cell.
Pathways
PDI1 is integral to the unfolded protein response (UPR) and protein folding pathway within the ER. During cellular stress PDI1 and other enzymes like BiP manage misfolded proteins preventing accumulation that could lead to ER stress. PDI1 also interacts with the calnexin/calreticulin cycle facilitating proper assembly of glycoproteins in conjunction with ERp72 ensuring that cellular pathways dependent on ER function proceed smoothly.
PDI1 is implicated in neurodegenerative disorders like Alzheimer's disease and cardiovascular diseases such as atherosclerosis. In Alzheimer's disease PDI1's impaired function may lead to the accumulation of misfolded proteins including amyloid beta. It interacts with other ER stress-related proteins like GRP78 in managing stress responses. In cardiovascular diseases PDI1's role in maintaining redox balance and protein folding can affect vascular health and integrity when disrupted and it works alongside proteins like atherogenic lipoproteins.