GRP78 / BIP Rabbit Polyclonal Antibody (R1401-26)

UNIPROT #

P11021

PROTEIN NAME

GRP78 / BIP

SYNONYMS

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

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 70 family.

POST-TRANSLATIONAL MODIFICATION

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).

SUBCELLULAR LOCATION

Endoplasmic reticulum lumen, melanosome. cytoplasm

FUNCTION

Binding immunoglobulin protein (BiP) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the HSPA5 gene. BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery, as well as playing a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. Like many stress and heat shock proteins, BiP/GRP78 has potent immunological activity when released from the internal environment of the cell into the extracelluar space.specifically, it feeds anti-inflammatory and pro-resolutory signals into immune networks, thus helping to resolve inflammation.