When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (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 (ER).

Endoplasmic reticulum chaperone BiP (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) HSPA5 GRP78

Human Mouse Rat

WB,IHC,ICC

WB 1:500~1:2000 IHC 1:50~1:200 ICC/IF 1:50~1:200

78kDa

HSPA5 GRP78

p11021

https://www.uniprot.org/uniprotkb/p11021

A synthesized peptide derived from human GRP78 BiP

Rabbit

Monoclonal

Rabbit IgG

GRP78 BiP Antibody detects endogenous levels of total GRP78 BiP

Affinity-chromatography

PBS, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.