Anti-GRP78, clone C19

Anti-GRP78, clone C19, Cat. No. MABS2159, is a mouse monoclonal antibody that detects the glycosylated form of GRP78 and has been tested for use in Flow Cytometry, Immunohistochemistry (Paraffin), and Immunoprecipitation.

Flow Cytometry Immunohistochemistry (Paraffin) Immunoprecipitation

Immunohistochemistry (Paraffin) Analysis: A representative lot detected glycosylated GRP78 in Immunohistochemistry applications (Moerkamp, A.T., et. al. (2017). Stem Cells Dev. 26(21):1552-1565).

Flow Cytometry Analysis: A representative lot detected glycosylated GRP78 in Flow Cytometry applications (Leung, H.W., et. al. (2015). J Mol Cell Cardiol. 82:228-37).

Immunoprecipitation Analysis: A representative lot immunoprecipitated glycosylated GRP78 in Immunoprecipitation applications (Leung, H.W., et. al. (2015). J Mol Cell Cardiol. 82:228-37).

Clone C19 is a mouse monoclonal antibody that specifically detects the glycosylated form of GRP78. Its reactivity is abolished upon deglycosylation.

1E07 Sca-1+ Cardiac progenitor cells isolated from human heart tissue.

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

Purified mouse monoclonal antibody IgM in PBS with 0.05% sodium azide.

Endoplasmic reticulum chaperone BiP (UniProt: P11021; also known as EC:3.6.4.10, 78 kDa glucose-regulated protein, GRP-78, Binding-immunoglobulin protein, BiP, Heat shock protein 70 family protein 5, HSP70 family protein 5, Heat shock protein family A member 5, Immunoglobulin heavy chain-binding protein) is encoded by the HSPA5 (also known as GRP78) gene (Gene ID: 3309) in human. GRP78 is an endoplasmic reticulum chaperone that can exist as a monomer and as a homooligomer. It plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It is involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5 and acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). It is synthesized with a signal peptide (aa 1-18), which is subsequently cleaved off to generate the mature form that contains a nucleotide-binding domain (NBD; aa 125-280), a substrate-binding domain (aa 420-500), and a short interdomain linker (aa 409-419). The interdomain linker regulates its chaperone activity by mediating it homo-oligomerization. Its chaperone activity is regulated by ATP-induced allosteric coupling of the NBD and substrate-binding domains. GRP78 expression is shown to be up-regulated during early cardiogenesis. Clone C19 recognizes glycosylated residues of GRP78 on cell surface of human cardiac progenitor cells and its de-N-glycosylation is shown to significantly abolish its binding. This clone displays strong staining on the majority of Sca-1+ cardiac progenitor cells, with negligible binding to hESCs and human fibroblast cells. (Ref.: Moerkamp, AT., et al. (2017). Stem Cell Dev. 26(21); 1252-1265; Leung, HW., et al. (2015). J. Mol. Cell. Cardiol. 82; 228-237).

Evaluated by Flow Cytometry in Jurkat cells.

Flow Cytometry Analysis: 1 µg of this antibody detected glycosylated GRP78 in one million Jurkat cells.

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