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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSPA5 (heat shock 70kDa protein 5) also known as glucose-regulated protein, 78kD (GRP78) or BiP, is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum. BiP is an essential component of the translocation machinery, as well as playing a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. Shen et al.(2002) concluded that BiP retains ATF6 in the ER by inhibiting its Golgi localization signals and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi. The findings of Shen et al.(2002) demonstrated that the protein is a key element in sensing the folding capacity within the ER.
For additional antibodies targeting BiP / 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 BiP antibody may be required due to differences in protocols and secondary/substrate sensitivity.
An amino acid sequence from the C-terminus of human GRP78/BiP (EWLESHQDADIEDFK) was used as the immunogen for this BiP antibody (100% homologous in human, mouse and rat).
After reconstitution, the BiP antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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