Lane 1: Mouse liver tissue
Lane 2: Rat liver tissue
Lane 3: HepG2
Rabbit polyclonal primary
GRP78 Rabbit Polyclonal Antibody (ER1706-50)
Synthetic peptide within n-terminal human grp78.
Mouse liver tissue lysate, rat liver tissue lysate, HepG2 cell lysate, A431, HepG2, HUVEC, rat brain tissue, human liver tissue, mouse cerebellum tissue, human placenta tissue, human stomach carcinoma tissue, Jurkat, Hela, SH-SY5Y.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified.
Predicted band size: 72 kDa
78 kDa glucose regulated protein antibody; 78 kDa glucose-regulated protein antibody; AL022860 antibody; AU019543 antibody; BIP antibody; D2Wsu141e antibody; D2Wsu17e antibody; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 antibody; Endoplasmic reticulum lumenal Ca2+ binding protein grp78 antibody; Epididymis secretory sperm binding protein Li 89n antibody; FLJ26106 antibody; Glucose Regulated Protein 78kDa antibody; GRP 78 antibody; GRP-78 antibody; GRP78 antibody; GRP78_HUMAN antibody; Heat shock 70 kDa protein 5 antibody; Heat Shock 70kDa Protein 5 antibody; Heat shock protein family A (Hsp70) member 5 antibody; HEL S 89n antibody; Hsce70 antibody; HSPA 5 antibody; HSPA5 antibody; Immunoglobulin Heavy Chain Binding Protein antibody; Immunoglobulin heavy chain-binding protein antibody; mBiP antibody; MIF2 antibody; Sez7 antibody
Belongs to the heat shock protein 70 family.
AMPylated by FICD. In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).
Endoplasmic reticulum. Cytoplasm.
Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity). GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP 75 and GRP 78 are unresponsive to heat stress and are induced by glucose deprivation.