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Product Details
MA5-47188
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human,
Mouse,
Rat
Host/Isotype
Rabbit
/ IgG
Expression System
HEK293 cells
Class
Recombinant Monoclonal
Type
Antibody
Clone
HL1815
Immunogen
Recombinant fragment of human Grp78
Conjugate
Form
Liquid
Concentration
1 mg/mL
Purification
Protein A
Storage buffer
PBS
Contains
no preservative
Storage conditions
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
Shipping conditions
Ambient (domestic); Wet ice (international)
RRID
AB_2938260
Product Specific Information
Store as concentrated solution.
Centrifuge briefly prior to opening vial.
Target Information
GRP78 is a 78 kDa glucose regulated protein that belongs to the family of heat shock proteins that include HSP70. GRP78 is a resident protein of the endoplasmic reticulum (ER) and associates transiently with a variety of newly synthesized secretory and membrane proteins. GRP78 may also interact with mutant and misfolded proteins, marking them for degradation. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C-terminus of GRP78 and other resident ER proteins including glucose regulated protein 94 (GRP94) and protein disulfide isomerase (PDI). The KDEL signal is recognized by the KDEL receptor and this interaction ensures recycling of escaped ER proteins back to the ER. GRP78’s involvement in correct folding of proteins and degradation of misfolded proteins is via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate. GRP78 is critical for maintenance of cell homeostasis and the prevention of apoptosis. GRP78 protein levels have been shown to be a reliable biomarker of hypoglycemia and serves a neuroprotective function in neurons exposed to glutamate and oxidative stress. GRP78 levels are reduced in the brains of Alzheimer's Disease patients, and decreased expression of GRP78 is found associated with missense mutations in the human presenilin-1 (PS1) gene. Further, the induction of the GRP78 protein has been associated with the development of drug-resistance to antitumor drugs.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: 78 kDa glucose-regulated protein; Binding-immunoglobulin protein; BiP; Endoplasmic reticulum chaperone BiP; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; epididymis secretory sperm binding protein Li 89n; FLJ26106; glucose regulated protein, 78 kDa; glucose-regulated protein, 78kDa; GRP 78; GRP-78; heat shock 70 kDa protein 5; heat shock 70kD protein 5; heat shock 70kD protein 5 (glucose-regulated protein, 78kD); heat shock 70kDa protein 5 (glucose-regulated protein); heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Heat shock protein 70 family protein 5; Heat shock protein family A member 5; HSP70 family protein 5; HSPA 5; Immunoglobulin heavy chain-binding protein; Steroidogenesis-activator polypeptide; XAP-1 antigen
Gene Aliases: AL022860; AU019543; baffled; BIP; D2Wsu141e; D2Wsu17e; GRP78; HEL-S-89n; Hsce70; HSPA5; mBiP; MIF2; SEZ-7; Sez7
UniProt ID: (Human) P11021, (Rat) P06761, (Mouse) P20029
Entrez Gene ID: (Human) 3309, (Rat) 25617, (Mouse) 14828
glycoprotein binding
calcium ion binding
protein binding
ATP binding
ATPase activity
enzyme binding
protein domain specific binding
ubiquitin protein ligase binding
ribosome binding
unfolded protein binding
chaperone binding
misfolded protein binding
cadherin binding involved in cell-cell adhesion
nucleotide binding
ER overload response
activation of signaling protein activity involved in unfolded protein response
cerebellum structural organization
cerebellar Purkinje cell layer development
substantia nigra development
positive regulation of cell migration
negative regulation of transforming growth factor beta receptor signaling pathway
positive regulation of protein ubiquitination
response to endoplasmic reticulum stress
maintenance of protein localization in endoplasmic reticulum
cellular response to glucose starvation
negative regulation of apoptotic process
proteolysis involved in cellular protein catabolic process
cellular response to antibiotic
cellular response to interleukin-4
toxin transport
positive regulation of embryonic development
ER-associated ubiquitin-dependent protein catabolic process
endoplasmic reticulum unfolded protein response
protein folding in endoplasmic reticulum
IRE1-mediated unfolded protein response
PERK-mediated unfolded protein response
ATF6-mediated unfolded protein response
regulation of protein folding in endoplasmic reticulum
cellular response to manganese ion
negative regulation of protein homodimerization activity
cell-cell adhesion
regulation of ATF6-mediated unfolded protein response
regulation of IRE1-mediated unfolded protein response
regulation of PERK-mediated unfolded protein response
positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
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