Journal: American Journal of Physiology - Renal Physiology

Article Title: Pharmacological and genetic inhibition of downstream targets of p38 MAPK in experimental nephrotic syndrome

doi: 10.1152/ajprenal.00207.2017

Figure Lengend Snippet: ADR-induced injury induced and activated small heat shock proteins (HSPs), primarily in an MK2-dependent manner. Total protein was extracted from renal cortexes isolated from control and ADR-injured mice on day 21 from each genotype and phosphorylated and total forms of HSPB1, HSPB8, glucose-regulated protein 78 (GRP78), and GAPDH were detected using their respective antibodies. A: representative Western blots of total and phosphorylated forms of selected proteins. B: densitometry analyses of protein induction/phosphorylation in the renal cortexes of at least 3 mice from each genotype. Statistical differences: *P < 0.05, control vs. ADR; #P < 0.05, WT-ADR treated vs. KO-ADR treated.

Article Snippet: The other primary antibodies used were anti-HSPB1 (StressMarq, Victoria, BC), anti-HSPB8 mouse monoclonal (Abcam, Cambridge, MA), anti-GRP78 rabbit monoclonal (StressMarq), and anti-GAPDH mouse monoclonal (Millipore, Billerica, MA).

Techniques: Isolation, Western Blot

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Box whisker plot showing relative mRNA expression of GRP78 in tumor tissue and adjacent non-tumor tissue of RCC patients. 18S was used as an internal control for normalization. Mann Whitney U Test was applied to determine significance. ∗∗∗p < 0.001.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Whisker Assay, Expressing, Control, MANN-WHITNEY

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Comparative expression of Glucose Related Protein 78 (GRP78) in RCC patients and controls.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing, Control, Concentration Assay

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Western blot image showing GRP78 protein expression in tumor tissue and adjacent non-tumor tissue of RCC patients. The representative image includes the information of three different tumor tissues and their respective adjacent non-tumor tissues of the stage 1(Fuhrman grade 2), stage 2(Fuhrman grade 3) and stage 3(Fuhrman grade 3) of clear cell RCC patients. β-actin was used as an internal control for normalization. (Supplementary Material, Western blot of GRP78 expression in tumor and adjacent non tumor tissue of RCC patients.)

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Western Blot, Expressing, Control

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Graph depicting relative fold intensity of GRP78 expression using Western blot assay in tumor tissue and adjacent non-tumor tissue of RCC patients. β-actin was used as an internal control for normalization. Mann Whitney Test was applied to determine significance. ∗∗∗p < 0.001.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing, Western Blot, Control, MANN-WHITNEY

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Representative images of GRP78 expression in adjacent non tumor tissue (A) and tumor tissue (B) of stage 3 (Fuhrman grade 3) of clear cell RCC patient studied using immunohistochemistry. All images were taken at 200 X magnification.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing, Immunohistochemistry

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Receiver Operating curve of serum GRP78 expression to discriminate between the presence or absence of RCC.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Box-whisker plot showing serum levels of GRP78 according to various pathological Tumor stage in RCC patients.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Whisker Assay

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Receiver Operating curve of serum GRP78 expression to discriminate between the presence or absence of metastasis.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Comparative expression of serum Glucose Regulated Protein 78(GRP78) in patients with clear cell RCC (RCC). ∗Significant at p < 0.05

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing, Histopathology

Journal: Heliyon

Article Title: Glucose- regulated protein 78 (GRP78) in renal cell carcinoma: A novel biomarker for predicting tumor behavior

doi: 10.1016/j.heliyon.2021.e07300

Figure Lengend Snippet: Receiver Operating curve of serum GRP78 expression to discriminate between low grade (Grade 1/Grade 2) versus High Grade (Grade 3/Grade 4) disease in RCC patients.

Article Snippet: Then the blot was incubated with GRP78 primary antibody (St John's Laboratory Ltd, London) (1:1000 dilution) overnight at room temperature followed by washing in TBS with 0.05% tween.

Techniques: Expressing

Journal: Frontiers in Pharmacology

Article Title: Licorice attenuates cisplatin-induced hepatotoxicity by alleviating endoplasmic reticulum stress and apoptosis

doi: 10.3389/fphar.2025.1557125

Figure Lengend Snippet: Gene primer sequences.

Article Snippet: WB analysis was performed as previously described ( ) using specific primary antibodies against CHOP (1:1000, 15204-1-AP, Proteintech), ATF4 (1:1000, BM5179, Boster), ATF6 (1:1000, A00655, Boster), GRP78 (1:1000, BA 2042, Boster), p-IRE1α (1:1000, NB100-2323, Novus), p-eIF2α (1:1000, BM3942, Boster), Bcl-2 (1:1000, A00040-1, Boster), Bax (1:1000, A00183, Boster), cleaved caspase-3 (1:1000, #9664T, Cell Signaling Technology), caspase-12 (1:1000, BA3142, Boster), cleaved caspase-8 (1:5000, ab108333, Abcam), p-PERK (1:1000, abs137056, Absin) and β-actin (1:5000, 20536-1-AP, Proteintech).

Techniques:

Journal: Frontiers in Pharmacology

Article Title: Licorice attenuates cisplatin-induced hepatotoxicity by alleviating endoplasmic reticulum stress and apoptosis

doi: 10.3389/fphar.2025.1557125

Figure Lengend Snippet: Effects of GC on CP-induced ER stress. (A) Effect of GC on the morphological changes of ER in liver cells induced by CP. Red arrows show the morphology of the endoplasmic reticulum and ribosomes. (B, C) Effect of GC on CP-induced ER stress-related indicators. GRP78, ATF6, and p-IRE1α protein expression were detected by WB analysis. GRP78 and ATF6 gene expression were detected by qRT-PCR analysis. All data are presented as the mean ± SD. ## p < 0.01 compared with control group; * p < 0.05, ** p < 0.01 compared with CP group.

Article Snippet: WB analysis was performed as previously described ( ) using specific primary antibodies against CHOP (1:1000, 15204-1-AP, Proteintech), ATF4 (1:1000, BM5179, Boster), ATF6 (1:1000, A00655, Boster), GRP78 (1:1000, BA 2042, Boster), p-IRE1α (1:1000, NB100-2323, Novus), p-eIF2α (1:1000, BM3942, Boster), Bcl-2 (1:1000, A00040-1, Boster), Bax (1:1000, A00183, Boster), cleaved caspase-3 (1:1000, #9664T, Cell Signaling Technology), caspase-12 (1:1000, BA3142, Boster), cleaved caspase-8 (1:5000, ab108333, Abcam), p-PERK (1:1000, abs137056, Absin) and β-actin (1:5000, 20536-1-AP, Proteintech).

Techniques: Expressing, Gene Expression, Quantitative RT-PCR, Control

Journal: Frontiers in Pharmacology

Article Title: Licorice attenuates cisplatin-induced hepatotoxicity by alleviating endoplasmic reticulum stress and apoptosis

doi: 10.3389/fphar.2025.1557125

Figure Lengend Snippet: (A-C) MTT assay for determining cell viability. (D-E) GC reduced the expression of ER stress-related indicators. Expression levels of GRP78, ATF6, and p-IRE1α protein were tested by WB analysis. Expression levels of GRP78 and ATF6 mRNA were tested by qRT-PCR analysis.

Article Snippet: WB analysis was performed as previously described ( ) using specific primary antibodies against CHOP (1:1000, 15204-1-AP, Proteintech), ATF4 (1:1000, BM5179, Boster), ATF6 (1:1000, A00655, Boster), GRP78 (1:1000, BA 2042, Boster), p-IRE1α (1:1000, NB100-2323, Novus), p-eIF2α (1:1000, BM3942, Boster), Bcl-2 (1:1000, A00040-1, Boster), Bax (1:1000, A00183, Boster), cleaved caspase-3 (1:1000, #9664T, Cell Signaling Technology), caspase-12 (1:1000, BA3142, Boster), cleaved caspase-8 (1:5000, ab108333, Abcam), p-PERK (1:1000, abs137056, Absin) and β-actin (1:5000, 20536-1-AP, Proteintech).

Techniques: MTT Assay, Expressing, Quantitative RT-PCR

Journal: Biology Open

Article Title: Endoplasmic reticulum stress-induced cellular dysfunction and cell death in insulin-producing cells results in diabetes-like phenotypes in Drosophila

doi: 10.1242/bio.046524

Figure Lengend Snippet: Induction of UPR observed in wing imaginal discs and IPCs with ectopic Hsc70-3 DN expression. (A–B) Expression of Xbp1-GFP generated by ER stress-dependent splicing of xbp1*-GFP mRNA in wing imaginal discs. Phase contrast (A,B) and fluorescence (A′,B′) micrographs of wing imaginal discs. (A,A′) Control wing disc ( Bx>xbp1*-GFP ). (B,B′) Wing disc expressing a dominant-negative form of Hsc70-3 in the wing pouch region (arrow) ( Bx>hsc70-3 DN , xbp1*-GFP ). (C–E) Fluorescence micrograph of wing discs stained with DAPI (white). (C′–E′) Immunostaining of the wing discs with an anti-GRP78 antibody. (D″) Immunostaining of the wing disc with anti-HA antibody. (C,C′) Fluorescence micrograph of a control wing imaginal disc ( Bx-Gal4/+ ). (D–D″) Wing imaginal disc expressing control Hsc70-3 in the wing pouch region of the imaginal disc ( Bx>hsc70-3 ). (E,E′) Wing imaginal disc expressing a dominant-negative form of Hsc70-3 in the same region ( Bx>hsc70-3 DN ). Anti-GRP78 immunostaining is shown in white. Note that more intense immunofluorescence was observed exclusively in areas expressing Hsc70-3 DN , but not the control protein. (A–F) Relative intensity of anti-GRP78 immunostaining in wing imaginal discs. Immunofluorescence signal intensity in each wing imaginal disc with the control Hsc70-3 ( n =31) or Hsc70-3 DN ( n =25) expression was calculated and normalized to the control value, which was set as 1.0 ( Bx-Gal4/+ ) ( n =25; n.s., not significant, P >0.05; *** P <0.001, Student's t -tests). Error bars represent s.e.m. (G–I) Anti-GRP78 immunostaining of IPCs expressing GFPnls in brains from third-instar larvae. (G) Control IPCs ( ilp2>GFPnls ), (H) IPCs expressing the control Hsc70-3 ( ilp2>hsc70-3, GFPnls ), (I) IPCs expressing Hsc70-3 DN ( ilp2>hsc70-3 DN , GFPnls ). Anti-GRP78 immunostaining is colored in red (G–I; white in G′–I′). Nuclei of IPCs visualized by GFPnls expression are colored green (G–I; white in G″–I″). Arrows in H′ and H″ indicate positions of IPC cells. Note that remarkably higher immunostaining signal was observed in IPCs expressing Hsc70-3 DN , but not the control protein. (J) Relative intensities of anti-GRP78 immunostaining in larval IPCs. Immunofluorescence signal intensities in each IPC expressing Hsc70-3 ( n =25) or Hsc70-3 DN ( n =21) were calculated and normalized to the control value of 1.0 ( ilp2>GFPnls ) ( n =21, * P <0.05, *** P <0.001, Student's t -test). Error bars represent s.e.m. Scale bars: (A–E) 100 µm, (G–I) 50 µm.

Article Snippet: The following primary antibodies were used at the dilution described; rabbit anti-β-galactosidase (MP Biomedicals, #55976) at 1:1000, rabbit anti-GRP78 (Bip) (StressMarq Biosciences Inc., Cadboro Bay, Victoria, Canada) that could recognize Hsp70 family proteins including Hsc70-3 in Drosophila at 1:500, rabbit Cleaved Caspase-3 (Asp175) (#9661, Cell Signaling, Danvers, Massachusetts, USA) at 1:200 for larval brain immunostaining and at 1:150 for wing disc immunostaining, rabbit anti-Cleaved Drosophila Dcp-1 (Asp216) (Cell Signaling, antibody #9578) at 1:500, and rabbit anti-phospho-SAPK/JNK (pThr183, pTyr185) (Calbiochem, La Jolla, CA, USA) at 1:200.

Techniques: Expressing, Generated, Fluorescence, Dominant Negative Mutation, Staining, Immunostaining, Immunofluorescence

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: (A) Effects of various HCV proteins on CAT expression driven by the grp78, grp94, or tk promoter in transient transfection into HuH-7 hepatoma cells. The results are normalized to CAT expression in the presence of pUC19 and are shown as the means and standard deviations from three transfections. (B) Effects of the individual HCV structural proteins on CAT expression driven by the grp78 or grp94 promoter in transient transfection into HuH-7 hepatoma cells. The results are normalized to CAT expression in the presence of pUC19 and are shown as the means and standard deviations from three transfections.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Expressing, Transfection

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: Immunofluorescence detection of GRP78 and E2 or E1 protein expression in HuH-7 cells transiently transfected with either the E2 (top) or E1 (bottom) expression plasmid. A low level of GRP78 is detectable in the untransfected cells, as revealed in the original photographs.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Immunofluorescence, Expressing, Transfection, Plasmid Preparation

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: Western blot detection of GRP78 and GRP94 in CHO cells (lane 1) or CHO cells stably expressing E2 protein (lane 2). Equal amounts of total cell extracts were separated by SDS-polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane for Western blotting against GRP78. The monoclonal antibody against GRP78 (StressGen SPA826) cross-reacts with GRP94. Numbers on the left are molecular weights in thousands.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Western Blot, Stable Transfection, Expressing, Polyacrylamide Gel Electrophoresis

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: Coimmunoprecipitation of E2 protein and GRP78. Proteins were immunoprecipitated from lysates of E2-expressing CHO cells with either of two different antibodies (Ab) to E2 protein (lanes 2 and 3) or an antibody to GRP78 (αGrp78) (lane 4), electrophoresed on an SDS-polyacrylamide gel, and probed for GRP78 by Western blotting. GRP78 was precipitated by all three antibodies; in contrast, no GRP78 was precipitated when the antibody was omitted (lane 1). Numbers on the left are molecular weights in thousands.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Immunoprecipitation, Expressing, Western Blot

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: Copurification of E2 protein and GRP78 in the absence but not the presence of Mg-ATP. Lysates from E2-expressing CHO cells were electrophoresed on an SDS-polyacrylamide gel and stained with Coomassie blue, either before (lanes 1 and 3) or after (lanes 2 and 4) chromatography on a GNA lectin column. In lanes 3 and 4, the lysate was preincubated with Mg-ATP for 15 min. Numbers on the left are molecular weights in thousands.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Copurification, Expressing, Staining, Chromatography

Journal:

Article Title: Activation of the grp78 and grp94 Promoters by Hepatitis C Virus E2 Envelope Protein

doi:

Figure Lengend Snippet: No evidence for copurification of E1 protein and GRP78. Lysates from E1-expressing CHO cells were electrophoresed on an SDS-polyacrylamide gel, transferred to a membrane, and probed for E1 protein (lanes 1 and 2) or GRP78 (lanes 3 and 4) by Western blotting, either before (lanes 1 and 3) or after (lanes 2 and 4) chromatography on a GNA lectin column. Numbers in the center are molecular weights in thousands.

Article Snippet: The membrane was analyzed by Western blotting with rabbit antibodies to GRP78 (StressGen SPA826), using the alkaline phosphatase (Promega) detection system.

Techniques: Copurification, Expressing, Western Blot, Chromatography

Journal: Investigative Ophthalmology & Visual Science

Article Title: In Search of the Identity of the XAP-1 Antigen: A Protein Localized to Cone Outer Segments

doi: 10.1167/iovs.09-4286

Figure Lengend Snippet: LC-MS/MS results obtained from the protein band corresponding to the XAP-1 antigen. (A) The MS/MS spectrum of a peptide from the LC-MS/MS analysis. It contains product ions of the b- and y- series that matched peptide sequence ITPSYVAFTPEGER from Grp78 from Mus musculus. (B) The m/z ratios for theoretical product ions of the y- and b- series. Product ions that were observed in the MS/MS spectrum are shown in bold.

Article Snippet: Blot A was incubated in rabbit anti-human Grp78 (1:1000 dilution; Anaspec) overnight at 4°C.

Techniques: Liquid Chromatography with Mass Spectroscopy, Tandem Mass Spectroscopy, Sequencing

Journal: Investigative Ophthalmology & Visual Science

Article Title: In Search of the Identity of the XAP-1 Antigen: A Protein Localized to Cone Outer Segments

doi: 10.1167/iovs.09-4286

Figure Lengend Snippet: Protein sequence of Mus musculus Grp78. The peptide from our MS/MS analysis is shown in gray text and represents 2.14% coverage.

Article Snippet: Blot A was incubated in rabbit anti-human Grp78 (1:1000 dilution; Anaspec) overnight at 4°C.

Techniques: Sequencing, Tandem Mass Spectroscopy

Journal: Investigative Ophthalmology & Visual Science

Article Title: In Search of the Identity of the XAP-1 Antigen: A Protein Localized to Cone Outer Segments

doi: 10.1167/iovs.09-4286

Figure Lengend Snippet: Depletion of IgM and Grp78 from the outer segment–enriched preparation. IgM and Grp78 were depleted from outer segment (OS) cell extracts. IgM and the XAP-1 antigen are shown in red, whereas Grp78 is shown in green. Overlap of the signals (E, F, yellow). A small amount of IgM was detected after one round of depletion, but none remained after a second round (A). Both the XAP-1 antigen (B) and Grp78 (C, D) remained in the sample after all IgM was removed. The XAP-1 antigen and Grp78 overlap at an identical relative molecular mass (F). Depletion of Grp78 (C, D) abolished the signal obtained with the XAP-1 antibody (B).

Article Snippet: Blot A was incubated in rabbit anti-human Grp78 (1:1000 dilution; Anaspec) overnight at 4°C.

Techniques:

Journal: Investigative Ophthalmology & Visual Science

Article Title: In Search of the Identity of the XAP-1 Antigen: A Protein Localized to Cone Outer Segments

doi: 10.1167/iovs.09-4286

Figure Lengend Snippet: Immunohistochemical localization of Grp78 in the retinas of mouse and frog. After antigen retrieval, retinas from C57BL6/J mice were immunostained using anti-Grp78 (A, green), PNA (B, red), and iodide (C, blue). (C) Composite image. Yellow (arrows) indicates areas of overlap of the Grp78 and PNA, indicating that in the outer retina, Grp78 is localized to cone photoreceptors in a pattern identical with that of the XAP-1 antigen. (C, inset) Higher magnification image of the area within the inset in C. In the mouse, Grp78 is also found in all cell layers of the retina in a location corresponding to ER. (D) Examination of the frog retina revealed a different pattern. The peripheries of both rod and cone photoreceptor outer segments and the inner segments are immunolabeled in this species. Scale bar, 10 μm. OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer.

Article Snippet: Blot A was incubated in rabbit anti-human Grp78 (1:1000 dilution; Anaspec) overnight at 4°C.

Techniques: Immunohistochemical staining, Immunolabeling