|Detection of Human GRP78/HSPA5 by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, Jurkat human acute T cell leukemia cell line, and MCF‑7 human breast cancer cell line. PVDF membrane was probed with 1 µg/mL of Human GRP78/HSPA5 Monoclonal Antibody (Catalog # MAB4846) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for GRP78/HSPA5 at approximately 78 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
Detection of Human GRP78/HSPA5 by Simple WesternTM. |
Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, loaded at 0.2 mg/mL. A specific band was detected for GRP78/HSPA5 at approximately 72 kDa (as indicated) using 10 µg/mL of Mouse Anti-Human GRP78/HSPA5 Monoclonal Antibody (Catalog # MAB4846). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
*Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.
GRP78 (Glucose-regulated protein 78 kDa; also BiP and HSPA5) is a 72 kDa member of the heat shock protein 70 family of proteins. Intracellularly, GRP78 is an endoplasmic reticulum chaperone that participates in protein folding; extracellularly, it induces IL-10 production from T cells and interacts with Cripto to block TGF-beta signaling. Human GRP78 precursor is 654 amino acids (aa) in length. It contains an 18 aa signal sequence and a 636 aa mature region that shows a hydantoinase A region (aa 145‑245) and a C-terminal KDEL motif that is present on intracellular GRP78, but absent on secreted GRP78. There is alternative splicing in the signal sequence (aa 1‑10), and multiple single aa substitituion. Over aa 1‑654, human GRP78 is more than 97% aa identical to mouse and rat GRP78.
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