- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSPA5 Antibody recognizes heat shock protein family A member 5, an endoplasmic reticulum molecular chaperone more commonly known as GRP78 or BiP. HSPA5 belongs to the HSP70 family of ATP-dependent protein-folding factors. The protein contains an amino-terminal nucleotide-binding domain, a substrate-binding domain and a carboxy-terminal KDEL retention sequence that supports localization within the endoplasmic reticulum. Cycles of ATP binding and hydrolysis regulate the interaction of HSPA5 with newly synthesized, incompletely assembled and misfolded proteins entering the secretory pathway.
Heat shock protein family A member 5 assists nascent proteins in achieving stable conformations and helps prevent the formation of inappropriate protein aggregates. HSPA5 can retain incompletely folded proteins within the endoplasmic reticulum and participate in directing terminally misfolded substrates toward endoplasmic reticulum-associated degradation. It is particularly important in professional secretory cells, including plasma cells, pancreatic cells and other cell types that produce large quantities of proteins for export. An HSPA5 Antibody can help researchers assess chaperone abundance and protein quality-control capacity in these metabolically active systems.
HSPA5 is also a major regulator of the unfolded protein response. In cells with low levels of endoplasmic reticulum stress, it associates with the luminal regions of PERK, IRE1 and ATF6. Accumulation of unfolded proteins draws HSPA5 away from these sensors, enabling activation of signaling programs that reduce protein-folding demand, increase chaperone expression and enhance removal of damaged proteins. These responses initially promote adaptation and recovery. If endoplasmic reticulum stress remains unresolved, prolonged signaling can instead contribute to inflammation, growth arrest or apoptosis.
Changes in HSPA5 expression have been examined in cancer, neurodegeneration, metabolic disorders, infection and inflammatory disease models. Increased abundance often reflects elevated secretory demand, nutrient deprivation, hypoxia or other conditions that disturb endoplasmic reticulum homeostasis. Researchers may use HSPA5 Antibody products in western blot, immunohistochemistry, immunofluorescence, flow cytometry or other validated applications to examine protein expression and localization. Analysis alongside CHOP, ATF4, XBP1, PERK or related markers can provide broader information about unfolded protein response activity. NSJ Bioreagents supplies HSPA5 Antibody options for research into HSP70-family chaperone function, protein quality control, cellular stress adaptation and endoplasmic reticulum signaling.
For additional antibodies targeting HSPA5, including products validated across multiple species and applications, visit our GRP78 Antibody page for endoplasmic reticulum stress and protein-folding research.
The stated application concentrations are suggested starting points. Titration of the HSPA5 Antibody / Heat Shock Protein Family A Member 5 Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Full length recombinant human protein was used as the immunogen for the HSPA5 Antibody.
Aliquot the HSPA5 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
GRP78 Antibody, BiP Antibody, Heat Shock Protein Family A Member 5 Antibody, Heat Shock 70 kDa Protein 5 Antibody, Glucose-Regulated Protein 78 Antibody, Endoplasmic Reticulum Chaperone BiP Antibody, Immunoglobulin Heavy Chain Binding Protein Antibody
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