GRP78 Antibody | Affinity Biosciences

Product:	GRP78 Antibody
Catalog:	AF5366
Description:	Rabbit polyclonal antibody to GRP78
Application:	WB IHC IF/ICC
Cited expt.:	WB, IHC
Reactivity:	Human, Mouse, Rat, Monkey
Prediction:	Rabbit, Chicken
Mol.Wt.:	60~100 kDa; 72kD(Calculated).
Uniprot:	P11021
RRID:	AB_2837851

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Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

Size	Price	Inventory
100ul	$280	In stock
200ul	$350	In stock

Lead Time: Same day delivery

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Related Downloads

MS Report

HPLC Report

MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Rabbit

Application:

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.

Reactivity:

Human,Mouse,Rat,Monkey

Prediction:

Rabbit(100%), Chicken(82%)

Clonality:

Polyclonal

Specificity:

GRP78 Antibody detects endogenous levels of total GRP78.

RRID:

AB_2837851
Cite Format: Affinity Biosciences Cat# AF5366, RRID:AB_2837851.

Conjugate:

Unconjugated.

Purification:

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

Storage:

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.

Alias:

Fold/Unfold

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;

Immunogens

Immunogen:

A synthesized peptide derived from human GRP78, corresponding to a region within C-terminal amino acids.

Uniprot:

P11021(BIP_HUMAN) >>Visit HPA database.

Gene(ID):

HSPA5(3309)

Description:

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).

Sequence:

P11021 BIP_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL

Predictions

Predictions:

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

Research Backgrounds

P11021_BIP_HUMAN

Function:

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).

Subcellular Location:

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

Family&Domains:

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.

Research Fields

· 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.

References

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). 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.

3). 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=6.9]

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).

4). 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=6.1]

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.

5). mTOR pathway mediates endoplasmic reticulum stress-induced CD4+ T cell apoptosis in septic mice. APOPTOSIS, 2022 (PubMed: 35759162) [IF=6.1]

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

6). 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.

7). Inhibition of ASIC1a-Mediated ERS Improves the Activation of HSCs and Copper Transport Under Copper Load. Frontiers in Pharmacology, 2021 (PubMed: 34135753) [IF=5.6]

Application: WB Species: Rat Sample: HSC-T6 cells

FIGURE 3 The effect of regulating the expression of ASIC1a on ERS in copper-treated HSC-T6 cells (A) Western blotting analysis and densitometric quantification of GRP78, and XBP1 protein levels in HSCs treated with PcTX-1; (B) mRNA levels of GRP78, and XBP1 in HSCs treated with PcTX-1 (C) Western blotting analysis and densitometric quantification of GRP78, XBP1 protein levels in HSCs transfected with ASIC1a-siRNA; (D) mRNA levels of GRP78, XBP1 in HSCs transfected with ASIC1a-siRNA. Statistical analyses were performed using t-test. Data are expressed as the mean ± SEM (n = 4). * p < 0.05, **p < 0.01 vs. Control group; # p < 0.05, ## p < 0.01 vs. CuSO4 group.

8). 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

9). Peroxisome Proliferator-Activated Receptor-Gamma Reduces ER Stress and Inflammation via Targeting NGBR Expression. Frontiers in Pharmacology, 2022 (PubMed: 35111067) [IF=5.6]

10). Thonningianin A ameliorates acetaminophen-induced liver injury by activating GPX4 and modulating endoplasmic reticulum stress. Frontiers in pharmacology, 2025 (PubMed: 40051561) [IF=5.6]

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GRP78 Antibody - #AF5366