Code | CSB-RA847116A0HU |
Size | US$210 |
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Application | Recommended Dilution |
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IHC | 1:50-1:200 |
CUSABIO isolated B lymphocytes from the animal immunized with a synthetic peptide derived from human HSPA5 and fused them with myeloma cells to generate hybridomas. The variable light and variable heavy domains of the HSPA5 antibody-producing hybridomas were sequenced for constructing a vector for a recombinant generation. The HSPA5 monoclonal antibody gene-containing vector was then transfected into cells and cultured to generate the HSPA5 recombinant monoclonal antibody. The HSPA5 recombinant monoclonal antibody was purified from the cell culture supernatant using affinity chromatography, and its specificity was verified through ELISA and IHC applications for human HSPA5 protein detection.
The HSPA5 protein, also known as GRP78 or BiP, is a chaperone protein that plays a key role in protein folding and quality control in the endoplasmic reticulum (ER) of cells. It is responsible for binding to and helping to fold newly synthesized proteins, as well as for recognizing and targeting misfolded or unfolded proteins for degradation. In addition to its chaperone functions, HSPA5 also serves as an important regulator of ER stress responses, helping to activate the unfolded protein response (UPR) pathway in response to ER stress. Dysfunction of HSPA5 and the UPR pathway has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic diseases.
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