- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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ERp57 Antibody / GRP58 Antibody recognizes ERp57, an endoplasmic reticulum protein encoded by the PDIA3 gene and also widely known as GRP58. ERp57 is a member of the protein disulfide isomerase family and participates in the formation, rearrangement and reduction of disulfide bonds during protein folding. Within the endoplasmic reticulum, ERp57 works closely with the lectin chaperones calnexin and calreticulin to promote the proper maturation of newly synthesized glycoproteins. These functions make ERp57 an important component of ER proteostasis and the cellular machinery responsible for maintaining protein quality control.
ERp57 contains thioredoxin-like domains that support oxidoreductase activity and interactions with partner proteins. Its association with calnexin and calreticulin directs ERp57 toward glycoprotein substrates undergoing folding in the ER lumen. By catalyzing disulfide bond formation and isomerization, GRP58 helps proteins achieve conformations compatible with normal trafficking and function. Proteins that fail to fold correctly can instead be retained within the ER and directed toward quality-control pathways, connecting ERp57 activity with broader mechanisms of proteostasis and cellular responses to protein-folding stress.
In addition to its role in glycoprotein folding, ERp57 contributes to antigen processing and presentation. PDIA3 is a component of the major histocompatibility complex class I peptide-loading complex, where it associates with proteins including tapasin and calreticulin. This complex facilitates the loading of antigenic peptides onto MHC class I molecules before their transport to the cell surface. An ERp57 Antibody can therefore support studies of both ER protein quality control and molecular mechanisms involved in antigen presentation and immune recognition.
GRP58 has also been investigated outside its classical ER-associated functions. PDIA3 has been detected in additional cellular compartments and has been linked to processes involving cellular stress responses, signaling and regulation of protein interactions. Changes in PDIA3 expression have been studied in cancer, neurobiology, metabolic disease and conditions associated with disrupted protein homeostasis. These diverse observations have expanded interest in ERp57 beyond its original characterization as an ER oxidoreductase while emphasizing the importance of cellular context when interpreting its biological functions.
ERp57 provides a useful molecular connection between protein folding, ER quality control and antigen presentation, making it relevant to broader studies of cellular proteostasis. Its cooperation with calnexin and calreticulin is particularly important for the maturation and quality control of glycoproteins within the secretory pathway. NSJ Bioreagents supplies antibodies to ERp57 and related proteins involved in protein folding and cellular homeostasis. An ERp57 Antibody can support research on GRP58, disulfide bond formation, ER proteostasis, glycoprotein folding and antigen processing.
For additional information on ERp57/GRP58 and its roles in protein folding, ER quality control and cellular proteostasis, see our PDIA3 Antibody page.
The stated application concentrations are suggested starting amounts. Titration of the ERp57 Antibody / GRP58 Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Amino acids 172-188 (LKAASNLRDNYRFAHTN) were used as the immunogen for this ERp57 antibody (100% homologous in human, mouse and rat).
After reconstitution, the ERp57 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
ERp57 antibody, GRP58 antibody, PDIA3 antibody, Protein Disulfide-Isomerase A3 antibody, 58 kDa Glucose-Regulated Protein antibody, ERp60 antibody
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