Anti-GRP78 Antibody, clone C38

72 kDa calculated

The gene HSPA5 encodes a protein named GRP-78 (78 kDa glucose-regulated protein) also known as BiP (immunoglobulin heavy chain-binding protein) or heat shock 70 kDa protein 5. While originally discovered as one of set of genes that were induced upon cellular starvation and stress, HSPA5 encoded GRP-78 is now known to be an important member of the heat-shock family of proteins. The HSPA5 encoded GRP-78 protein appears to play a role in helping in the assembly of multimeric protein complexes in the endoplasmic reticulum (ER). Cellular localization is in the endoplasmic reticulum lumen and appears as cytoplasmic-like staining. The HSPA5 encoded protein is an essential component of the translocation processes within the endoplasmic reticulum and also functions in the retrograde transport across the ER membrane of incorrectly folded proteins destined to be degraded by the ubiquitin proteasome system. The HSPA5 encoded protein, while widely expressed in all cells types under normal conditions, is particularly induced under conditions of cellular stress, heat, or toxins and conditions which lead to the accumulation of unfolded proteins in the ER.

Recombinant protein corresponding to human GRP78.

Research Category
Signaling

Research Sub Category
Insulin/Energy Signaling

Flow Cytometry Analysis: A representative lot from an independent laboratory detected GRP78 in HepG2 cells (de Ridder, G. G., et al. (2012). Melanoma Res. 22(3):225-235.).

Anti-GRP78 Antibody, clone C38 detects level of GRP78 & has been published & validated for use in GRP78.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2bκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Evaluated by Flow Cytometry in HeLa cells.

Flow Cytometry Analysis: 1 µg of this antibody detected GRP78 in 1X10E6 HeLa cells.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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