Molecular Classification
Molecular chaperone, Heat shock protein, ER stress response protein
Other Names
GRP-78, HSPA5, 78 kDa glucose-regulated protein, Heat shock 70 kDa protein 5
Disease Roles
CancerAutoimmune diseasesInflammation

Binding Immunoglobulin Protein Overview

Binding immunoglobulin protein (BiP), also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5), is a molecular chaperone located primarily in the lumen of the endoplasmic reticulum (ER). It plays a central role in protein folding, quality control, and ER stress response mechanisms. It also modulates immune responses through interactions with various immune cells.

Mechanism of Action

Modulation of protein folding, ATP hydrolysis, and interaction with immune cell receptors.

Biological Functions

Protein folding
ER quality control
ER stress response
Chaperone activity
Immune modulation

Disease Associations

Cancer
Autoimmune diseases
Inflammation
Neurodegenerative diseases
Other

Safety Considerations

  • Potential for altered cellular stress resistance
  • Possible role as an autoantigen in autoimmune diseases

Interacting Drugs

Calcium ionophores
Tunicamycin

Associated Biomarkers

Biomarker
Expression levels of BiP as a marker of ER stress
Surface BiP as a marker of autoimmune activity