GRP78 Antibody | Affinity Biosciences

製品:	GRP78 Antibody
カタログ:	AF5366
タンパク質の説明:	Rabbit polyclonal antibody to GRP78
アプリケーション:	WB IHC IF/ICC
反応性:	Human, Mouse, Rat, Monkey
予測:	Rabbit, Chicken
分子量:	60~100 kDa; 72kD(Calculated).
ユニプロット:	P11021
RRID:	AB_2837851

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サイズ	価格	在庫状況
100ul	$280	在庫あり
200ul	$350	在庫あり

プロトコル

製品説明

ソース:

Rabbit

アプリケーション:

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

反応性:

Human,Mouse,Rat,Monkey

予測:

Rabbit(100%), Chicken(82%)

クローナリティ:

Polyclonal

特異性:

GRP78 Antibody detects endogenous levels of total GRP78.

RRID:

AB_2837851
引用形式: Affinity Biosciences Cat# AF5366, RRID:AB_2837851.

コンジュゲート:

Unconjugated.

精製:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

保存:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

別名:

折りたたみ／展開

78 kDa glucose regulated protein; 78 kDa glucose-regulated protein; AL022860; AU019543; BIP; D2Wsu141e; D2Wsu17e; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; Epididymis secretory sperm binding protein Li 89n; FLJ26106; Glucose Regulated Protein 78kDa; GRP 78; GRP-78; GRP78; GRP78_HUMAN; Heat shock 70 kDa protein 5; Heat Shock 70kDa Protein 5; Heat shock protein family A (Hsp70) member 5; HEL S 89n; Hsce70; HSPA 5; HSPA5; Immunoglobulin Heavy Chain Binding Protein; Immunoglobulin heavy chain-binding protein; mBiP; MIF2; Sez7;

免疫原

免疫原:

Uniprot:

P11021(BIP_HUMAN) >>Visit HPA database.

遺伝子(ID):

HSPA5(3309)

タンパク質の説明:

GRP78 a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells.. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK).

タンパク質配列:

P11021 BIP_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL

種類予測

種類予測:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species

Results

Score

Rabbit

100

Chicken

Bovine

Dog

Zebrafish

Xenopus

Pig

Horse

Sheep

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P11021 基板として

P11021

Site	PTM Type	Enzyme	Source
S4	Phosphorylation		Uniprot
S14	Phosphorylation		Uniprot
T37	Phosphorylation		Uniprot
Y39	Phosphorylation		Uniprot
R60	Methylation		Uniprot
S64	Phosphorylation		Uniprot
Y65	Phosphorylation		Uniprot
T69	O-Glycosylation		Uniprot
T69	Phosphorylation		Uniprot
K81	Ubiquitination		Uniprot
T85	Phosphorylation		Uniprot
S86	Phosphorylation		Uniprot
T91	Phosphorylation		Uniprot
K96	Acetylation		Uniprot
K96	Ubiquitination		Uniprot
S107	Phosphorylation		Uniprot
K113	Acetylation		Uniprot
K113	Ubiquitination		Uniprot
K118	Acetylation		Uniprot
K118	Ubiquitination		Uniprot
K122	Acetylation		Uniprot
K123	Acetylation		Uniprot
K123	Ubiquitination		Uniprot
K125	Acetylation		Uniprot
K125	Ubiquitination		Uniprot
Y127	Phosphorylation		Uniprot
K138	Acetylation		Uniprot
K138	Ubiquitination		Uniprot
T139	Phosphorylation		Uniprot
S146	Phosphorylation		Uniprot
K152	Acetylation		Uniprot
K152	Ubiquitination		Uniprot
K154	Acetylation		Uniprot
K154	Ubiquitination		Uniprot
Y160	Phosphorylation		Uniprot
K163	Acetylation		Uniprot
K163	Ubiquitination		Uniprot
K164	Ubiquitination		Uniprot
Y175	Phosphorylation		Uniprot
K185	Ubiquitination		Uniprot
T189	Phosphorylation		Uniprot
R197	Methylation		Uniprot
T203	O-Glycosylation		Uniprot
T203	Phosphorylation		Uniprot
Y209	Phosphorylation		Uniprot
K213	Ubiquitination		Uniprot
T229	Phosphorylation	P11021 (HSPA5)	Uniprot
K268	Acetylation		Uniprot
K268	Methylation		Uniprot
K268	Ubiquitination		Uniprot
S311	Phosphorylation		Uniprot
Y313	Phosphorylation		Uniprot
S319	Phosphorylation		Uniprot
K326	Acetylation		Uniprot
K326	Ubiquitination		Uniprot
K340	Acetylation		Uniprot
K340	Ubiquitination		Uniprot
K344	Ubiquitination		Uniprot
K352	Acetylation		Uniprot
K352	Sumoylation		Uniprot
K352	Ubiquitination		Uniprot
K353	Acetylation		Uniprot
K353	Sumoylation		Uniprot
K353	Ubiquitination		Uniprot
S354	Phosphorylation		Uniprot
S365	Phosphorylation		Uniprot
T366	Phosphorylation		Uniprot
K370	Ubiquitination		Uniprot
K376	Acetylation		Uniprot
K376	Ubiquitination		Uniprot
K382	Ubiquitination		Uniprot
T441	Phosphorylation		Uniprot
K447	Ubiquitination		Uniprot
S448	Phosphorylation		Uniprot
S452	Phosphorylation		Uniprot
T453	Phosphorylation		Uniprot
S455	Phosphorylation		Uniprot
T460	Phosphorylation		Uniprot
K464	Ubiquitination		Uniprot
Y466	Phosphorylation		Uniprot
K474	Ubiquitination		Uniprot
T485	Phosphorylation		Uniprot
R492	Methylation		Uniprot
T518	Phosphorylation		Uniprot
K523	Ubiquitination		Uniprot
T525	Phosphorylation		Uniprot
T527	Phosphorylation		Uniprot
K547	Acetylation		Uniprot
K547	Ubiquitination		Uniprot
S567	Phosphorylation		Uniprot
Y568	Phosphorylation		Uniprot
Y570	Phosphorylation		Uniprot
S571	Phosphorylation		Uniprot
K573	Ubiquitination		Uniprot
K579	Acetylation		Uniprot
K581	Methylation		Uniprot
K585	Acetylation		Uniprot
K585	Methylation		Uniprot
K585	Ubiquitination		Uniprot
S587	Phosphorylation		Uniprot
S588	Phosphorylation		Uniprot
K591	Methylation		Uniprot
K596	Methylation		Uniprot
K601	Acetylation		Uniprot
K601	Ubiquitination		Uniprot
S607	Phosphorylation		Uniprot
K617	Acetylation		Uniprot
K617	Ubiquitination		Uniprot
K619	Acetylation		Uniprot
S632	Phosphorylation		Uniprot
K633	Acetylation		Uniprot
K633	Ubiquitination		Uniprot
Y635	Phosphorylation		Uniprot
S637	Phosphorylation		Uniprot
T643	O-Glycosylation		Uniprot
T643	Phosphorylation		Uniprot
T648	Phosphorylation		Uniprot
K651	Acetylation		Uniprot

PTMs - P11021 酵素として

P11021

Substrate	Site	Source
P11021 (HSPA5)	T229	Uniprot

研究背景

P11021_BIP_HUMAN

機能:

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.

PTMs:

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).

細胞の位置付け:

Endoplasmic reticulum lumen. Melanosome. Cytoplasm.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

サブユニット構造:

Monomer and homooligomer; homooligomerization via the interdomain linker inactivates the chaperone activity and acts as a storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC1 (via J domain) (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts with DNAJC10. Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (By similarity). Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (By similarity). Interacts with METTL23. Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration. Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum. Interacts with CIPC. Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis. Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum. Interacts with MANF; the interaction is direct. Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response. Interacts with CLU under stressed condition; interaction increases CLU protein stability; facilitates its retrotranslocation and redistribution to the mitochondria; cooperatively suppress stress-induced apoptosis by stabilizing mitochondrial membrane integrity. Interacts with CCDC47 (By similarity).

タンパク質ファミリー:

The interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers.

Belongs to the heat shock protein 70 family.

研究領域

· Genetic Information Processing > Folding, sorting and degradation > Protein export.

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum. (View pathway)

· Human Diseases > Neurodegenerative diseases > Prion diseases.

· Organismal Systems > Immune system > Antigen processing and presentation. (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone synthesis.

参考文献

1). TRAIL‐Armed ER Nanosomes Induce Drastically Enhanced Apoptosis in Resistant Tumor in Combination with the Antagonist of IAPs (AZD5582). Advanced Healthcare Materials, 2021 (PubMed: 33963815) [IF=10.0]

2). Epimedin B exerts neuroprotective effect against MPTP-induced mouse model of Parkinson's disease: GPER as a potential target. Biomedicine & Pharmacotherapy, 2022 (PubMed: 36411637) [IF=7.5]

Application: WB Species: Mouse Sample:

Fig. 7. Epimedin B exerts anti-apoptotic and anti-endoplasmic reticulum stress effects on MPTP-induced PD mice through GPER. Western blot assay was used to assess the effect of Epimedin B on the protein expressions of apoptosis-related protein Bax and Bcl-2 (A), and endoplasmic reticulum stress-related protein GRP78 and CHOP (B). Data are expressed as means ± SD, (n = 6).

3). mTOR pathway mediates endoplasmic reticulum stress-induced CD4+ T cell apoptosis in septic mice. APOPTOSIS, 2022 (PubMed: 35759162) [IF=7.2]

Application: WB Species: Mice Sample: CD4+ T cells

Fig. 4 Expression of ERS-UPR- and mTOR-related proteins in splenic CD4+ T cells of septic mice. Protein expression of GRP78, CHOP, mTOR, p-mTOR, p70S6k, p-p70S6k (A–E) in CD4+ T cells were quantified by western blotting and showed as the relative expression values of β-actin, which was used as a loading control to normalize the protein levels. In order to highlight the activation level of p-mTOR and p-p70S6K in this signaling pathway, the ratio of p-mTOR to mTOR (p/t mTOR) and p-p70S6K to p70S6K (p/t p70S6K) were used for statistics. Data are shown as Mean ± SD (n = 6). Statistically significant differences were determined by two-tailed Student’s t-test. **P < 0.01, ***P < 0.001, ****P < 0.0001

4). Aqueous Extract of Pepino Leaves Ameliorates Palmitic Acid-Induced Hepatocellular Lipotoxicity via Inhibition of Endoplasmic Reticulum Stress and Apoptosis. Antioxidants, 2021 (PubMed: 34204987) [IF=7.0]

Application: WB Species: Human Sample: HepG2 Cells

Figure 5 AEPL attenuated ER stress while PA exposure. (a) ER stress-related protein levels were analyzed by Western blotting. (b–d) GRP78, phosphorylated PERK, and phosphorylated IRE1αwere normalized to PERK, IRE1α, and β-actin of each sample. (e) SREBP-1 level in each group was normalized to β-actin. All data were presented as mean ± SD of at least three independent experiments. * p < 0.05 vs. control cells; # p < 0.05 vs. PA-treated cells.

5). The role of vitamin E in polyunsaturated fatty acid synthesis and alleviating endoplasmic reticulum stress in sub-adult grass carp (Ctenopharyngodon idella). Animal nutrition (Zhongguo xu mu shou yi xue hui), 2024 (PubMed: 38371478) [IF=6.3]

Application: WB Species: fish Sample:

Fig. 5 Effects of vitamin E on the relative protein expressions of endoplasmic reticulum stress-related proteins in the muscle of sub-adult grass carp. (A) Western blots for p-PERK (Ser1096), p-IRE1 (Ser724), ATF6 and GRP78. Quantification of (B) p-PERK (Ser1096), (C) p-IRE1 (Ser724), (D) ATF6, and (E) GRP78 normalized to β-actin. Results are represented as the mean ± SD. The data are the means of three replicates with two fishes per replicate (n = 3). Mean values within the same row with different superscripts are significantly different (P < 0.05). p-PERK (Ser1096) = protein kinase R-like endoplasmic reticulum kinase (phospho-Ser1096); p-IRE1 (Ser724) = inositol-requiring enzyme 1 (phospho-Ser724); ATF6 = activating transcription factor 6; GRP78 = glucose regulatory protein 78.

6). The role of SUMO specific peptidase 3 in secondary inflammation of ischemic stroke in mice. Biochimica et biophysica acta. Molecular basis of disease, 2024 (PubMed: 38437993) [IF=6.2]

7). Sesamol supplementation alleviates nonalcoholic steatohepatitis and atherosclerosis in high-fat, high carbohydrate and high-cholesterol diet-fed rats. Food & Function, 2021 (PubMed: 34606548) [IF=6.1]

Application: WB Species: Rat Sample:

Fig. 5 Sesamol regulated the hepatic ERS-IRE1 signaling pathway and NLRP3 expression in HF-HCC diet-fed rats. (A) Representative images of the western blot analyses from hepatic Bip, IRE1, phospho-IRE1, and NLRP3 expression. (B) The semi-quantitative analysis of Bip, and (C and D) representative images of the IHC analyses from hepatic phospho-IRE1 and NLRP3 expression (samples from 3 rats in each group were analyzed). Values are expressed as means ± SEM (n = 3); ###P < 0.001, versus control; ***P < 0.001, versus HF-HCC.

8). GnRHa protects the ovarian reserve by reducing endoplasmic reticulum stress during cyclophosphamide-based chemotherapy. npj Breast Cancer, 2021 (PubMed: 34620881) [IF=5.9]

Application: WB Species: Human Sample: KGN cells

Fig. 3 Cyclophosphamide inhibits AMH secretion in vitro. a Representative western blot analysis of GRP78 and AMH from KGN cells at 36 h and 48 h after injection of vehicle or CTX at doses of 250–1250 µg/mL. b Apoptosis assay of KGN cells 36 h and 48 h after injection of vehicle or CTX at doses of 250–1250 µg/mL. Compared with untreated control cells, the level of apoptosis was significantly higher with ≥750 µg/mL CTX. c, d AMH mRNA levels of KGN cells verified by qPCR. e, f The concentration of AMH in the cell-culture medium declined as the CTX dose increased. g, h One-way ANOVA analysis of apoptotic cells displayed on b. All error bars represent the standard error of the mean. *P < 0.05, **P < 0.001, and ***P < 0.0001.

9). The potential immunotoxicity of fine particulate matter based on SD rat spleen. ENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH, 2019 (PubMed: 31218585) [IF=5.8]

Application: WB Species: rat Sample: spleen

Fig. 3 | PM2.5 induced ERS in spleen of SD rats. a, b The levels of spleen GRP78 and ATF6 mRNA were measured using qRT-PCR by summer and winter PM2.5 treatment in SD rat. c, dThe levels of spleen GRP78 and ATF6 protein were measured using western blotting in summer PM2.5 treatment in SD rats and quantification of analysis

10). Protective Effect of Patchouli Alcohol Against High-Fat Diet Induced Hepatic Steatosis by Alleviating Endoplasmic Reticulum Stress and Regulating VLDL Metabolism in Rats. Frontiers in Pharmacology, 2019 (PubMed: 31632274) [IF=5.6]

Application: WB Species: rat Sample: liver

FIGURE 4 | PA treatment attenuated HFD-induced ER stress in rats. (A) Representative immunoreactive bands of GRP78, PERK, p-PERK, IRE1α, p-IRE1α, and ATF6

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GRP78 Antibody - #AF5366

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