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Invitrogen
GRP78 Polyclonal Antibody
高级验证
This Antibody was verified by Cell treatment to ensure that the antibody binds to the antigen stated.
产品信息
PA5-32437
应用
建议稀释比
已发表文章
产品规格
种属反应
Chicken,
Human,
Mouse
已发表种属
Rat
宿主/亚型
Rabbit
/ IgG
分类
Polyclonal
类型
Antibody
抗原
Synthetic peptide corresponding to near N-terminus of human GRP78
偶联物
形式
Liquid
纯化类型
Antigen affinity chromatography
保存液
PBS, pH 7.6, with 1% BSA
内含物
0.1% sodium azide
保存条件
-20° C, Avoid Freeze/Thaw Cycles
运输条件
Ambient (domestic); Wet ice (international)
RRID
AB_2549906
产品详细信息
This antibody is predicted to react with bovine, chicken, canine, amphibian, mouse and rat based on sequence homology.
Heat-mediated antigen retrieval is recommended prior to staining, using a 10mM citrate buffer, pH 6.0, for 10 minutes followed by cooling at room temperature for 20 min. Following antigen retrieval, incubate samples with primary antibody for 10 min at room temperature. A suggested positive control is breast carcinoma.
靶标信息
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
生物信息学
蛋白别名: 78 kDa glucose-regulated protein; 78-kD glucose-regulated protein precursor; 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; heat shock 70 kDa protein 5; heat shock 70kD protein 5 (glucose-regulated protein, 78kD); 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; XAP-1 antigen
基因别名: AL022860; AU019543; baffled; BIP; D2Wsu141e; D2Wsu17e; GRP78; HEL-S-89n; Hsce70; HSPA5; mBiP; MIF2; SEZ-7; Sez7
UniProt ID: (Chicken) Q90593, (Human) P11021, (Mouse) P20029
Entrez Gene ID: (Chicken) 396487, (Human) 3309, (Mouse) 14828
protein binding
ATP binding
ATPase activity
heat shock protein binding
protein binding involved in protein folding
unfolded protein binding
misfolded protein binding
glycoprotein binding
calcium ion binding
enzyme binding
protein domain specific binding
ubiquitin protein ligase binding
ribosome binding
chaperone 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
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
positive regulation of embryonic development
cellular response to glucose starvation
negative regulation of apoptotic process
proteolysis involved in cellular protein catabolic process
cellular response to interleukin-4
toxin transport
response to unfolded protein
ER-associated ubiquitin-dependent protein catabolic process
endoplasmic reticulum unfolded protein response
negative regulation of protein complex assembly
cellular response to unfolded protein
protein refolding
chaperone mediated protein folding requiring cofactor
negative regulation of IRE1-mediated unfolded protein response
substantia nigra development
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 antibiotic
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
