Journal: Cell reports

Article Title: Xbp1-independent Ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila

doi: 10.1016/j.celrep.2013.09.046

Figure Lengend Snippet: Ire1 is required for Rh1 delivery into the rhabdomere. (A) 72 h pupal eye with eyeless-Flipase induced clones of PBac{WH}Ire1f02170 homozygous cells, labeled by the absence of myrGFP (green), show defective delivery of Rh1 (blue) into the rhabdomeres (actin, red). The magnified mutant and control ommatidia are indicated with white squares. (B) Rh1 (blue) delivery into the rhabdomeres is normal in clones of a precise excision of PBac{WH}Ire1f02170 (labeled by the absence of myrGFP, green). (C) GMR-Gal4>UAS-Ire1 expression rescues Rh1 (blue) delivery into the rhabdomeres of PBac{WH}Ire1f02170 homozygous cells (labeled by the absence of DsRed). (D) The CH322-07H05 genomic construct rescues Rh1 (blue) delivery into the rhabdomeres of PBac{WH}Ire1f02170 homozygous cells (absence of myrGFP, green). (E–G) PBac{WH}Ire1f02170 homozygous cells (absence of myrGFP, green) have reduced levels (arrows) of (E) BiP/GRP78 (blue and monochrome) and (F) ninaA (blue and monochrome), but not (G) Cnx (blue and monochrome). (H) Western blot analysis of Rh1 mature (34 kDa) and immature (40 kDa) forms from adult head protein extracts of yw (WT, positive control), FRT82BPBac{WH}Ire1f02170/FRT82BCL,GMR-hid (whole eye is composed of homozygous Ire1 mutant cells as in (Stowers and Schwarz, 1999)), ninaE17 (Rh1 protein null) and 2 ninaA mutations (ninaA1=ninaAP228 and ninaAE110V). Tubulin is used as loading control. Scale bars, 10 μm.

Article Snippet: Primary antibodies were as follows: rat anti-ELAV (7E8A10, DSHB), guinea pig anti-homothorax ( Wildonger et al., 2005 ), guinea pig anti-Runt ( Duffy et al., 1991 ), rat anti-cadherin (DCAD2, DSHB), mouse anti-armadillo (N2 7A1, DSHB), rabbit anti-aPKC (Santa Cruz, sc-216), mouse anti-Crumbs (Cq4, DSHB), mouse anti-spam (21A6, DSHB), mouse anti-Rh1 (4C5, DSHB), mouse anti-tubulin (12G10, DSHB), guinea pig anti-Bip/GRP78 (Hsc-3) ( Ryoo et al., 2007 ), rabbit anti-Bip/GRP78 (StressMarq Biosciences, SPC-180), guinea pig anti-ATF4 ( Kang et al., 2012 ), rabbit anti-calnexin ( Rosenbaum et al., 2006 ), rabbit anti-ninaA ( Baker et al., 1994 ), rabbit anti-Pdi (Abcam, ab2792), rabbit anti-fatp ( Dourlen et al., 2012 ) and mouse anti-Sparc ( Portela et al., 2010 ).

Techniques: Clone Assay, Labeling, Mutagenesis, Expressing, Construct, Western Blot, Positive Control

Journal: Cell reports

Article Title: Xbp1-independent Ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila

doi: 10.1016/j.celrep.2013.09.046

Figure Lengend Snippet: Xbp1 is not required for Spacemaker/Eyes shut secretion or Rh1 delivery into the rhabdomere. (A) Schematic of Xbp1 genomic region with the localization of P[lacW]Xbp1K13803, P[PTT-GB]Xbp1CB02061and P[SUPor-P]CG9418KG05183. Excisions 81 and 79 delete the DNA binding domain of Xbp1 and were generated from jumps of P[PTT-GB]Xbp1CB02061. In excision 81, the sequence from 4bp to 622bp downstream from Xbp1 start codon (ATG) is deleted. In excision 79, the sequence between 260bp upstream and 748bp downstream from Xbp1 start codon (ATG) is deleted. In excision 250, the open reading frame of Xbp1 is deleted from 5bp after the start codon, together with CG9418 and CG15657, until 2R:17036107, in the inter-genic region between CG15657 and CG30389. Excision 250 was generated from a jump of P[SUPor-P]CG9418KG05183. (B) By 62 h pupation, eyeless-Flipase induced clones of cells homozygous for Excision 79, labeled by the absence of myrGFP (green), have normal levels of Spam/Eys (blue) in the IRS. The rhabdomeres are stained with actin (red). (C) At 72 h. pupa, Rh1 (blue) is delivered to the rhabdomere in photoreceptors homozygous for Excision 79, labeled by the absence of myrRFP (red), but Xbp1 mutant photoreceptors have lower levels of Rh1 in the rhabdomere in than wild type (monochrome magnifications with wild type and mutant ommatidia). (D) At 82 h. pupa, photoreceptors homozygous for Excision 79 present higher levels of Rh1 in the rhabdomere than wild-type. Excision 79 homozygous photoreceptors show even distribution of Rh1 in the rhabdomere, while wild-type show the typical crescent-shaped gradient of concentration with higher levels at the rhabdomere base (monochrome magnifications). (E) Quantification of Rh1 intensity. Average of the ratio of Rh1 fluorescence intensity divided by respective area between pairs of adjacent Excision 79 homozygous and wild-type ommatidia, at 72 and 82 hours of pupal development (FluoEx79/AreaEx79/FluoWT/AreaWT). Around 70 pairs of Excision 79 homozygous and wild-type ommatidia were quantified at each time point. At 72 h. pupa, Excision 79 homozygous photoreceptors have reduced levels of (F) BiP/GRP78 (blue and monochrome) and (G) ninaA (blue and monochrome) but not (H) Cnx (blue and monochrome). Scale bars, 10 μm.

Article Snippet: Primary antibodies were as follows: rat anti-ELAV (7E8A10, DSHB), guinea pig anti-homothorax ( Wildonger et al., 2005 ), guinea pig anti-Runt ( Duffy et al., 1991 ), rat anti-cadherin (DCAD2, DSHB), mouse anti-armadillo (N2 7A1, DSHB), rabbit anti-aPKC (Santa Cruz, sc-216), mouse anti-Crumbs (Cq4, DSHB), mouse anti-spam (21A6, DSHB), mouse anti-Rh1 (4C5, DSHB), mouse anti-tubulin (12G10, DSHB), guinea pig anti-Bip/GRP78 (Hsc-3) ( Ryoo et al., 2007 ), rabbit anti-Bip/GRP78 (StressMarq Biosciences, SPC-180), guinea pig anti-ATF4 ( Kang et al., 2012 ), rabbit anti-calnexin ( Rosenbaum et al., 2006 ), rabbit anti-ninaA ( Baker et al., 1994 ), rabbit anti-Pdi (Abcam, ab2792), rabbit anti-fatp ( Dourlen et al., 2012 ) and mouse anti-Sparc ( Portela et al., 2010 ).

Techniques: Binding Assay, Generated, Sequencing, Clone Assay, Labeling, Staining, Mutagenesis, Concentration Assay, Fluorescence

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

Article Title: Marchantin M Induces Apoptosis of Prostate Cancer Cells Through Endoplasmic Reticulum Stress

doi: 10.12659/MSM.894476

Figure Lengend Snippet: Marchantin effect on PC-3 cell apoptosis. Thirty days after the treatment of Marchantin, PC-3 cell apoptosis was measured by flow cytometry. * P<0.05, ** P<0.01, compared with group A and B; # P<0.05, ## P<0.01, compared with group E; & P<0.05, && P<0.01, compared with group D; $ P<0.05, $$ P<0.01, compared with group C. A: Control (Saline); B: DMSO; C: Higher dose of marchantin (200 μmol/kg); D: Medium dose of marchantin (100 μmol/kg); E: Lower dose of marchantin (50 μmol/kg).

Article Snippet: Dimethyl sulfoxide was bought from Xi’an Tianzheng Co., LTD. TUNEL apoptosis detection kit, CHOPm and GRP78 monoclonal antibody, and CHOP and GRP78 immunohistochemistry kits were supplied by the Wuhan Boster Biotechnology Co., LTD.

Techniques: Flow Cytometry, Control, Saline

Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

Article Title: Marchantin M Induces Apoptosis of Prostate Cancer Cells Through Endoplasmic Reticulum Stress

doi: 10.12659/MSM.894476

Figure Lengend Snippet: Effect of marchantin on DU145 cell apoptosis. Thirty days after the treatment of Marchantin, DU145 cell apoptosis was measured by flow cytometry. * P<0.05, compared with group A; # P<0.05, compared with 5μmol/L group. A: Control (Saline).

Article Snippet: Dimethyl sulfoxide was bought from Xi’an Tianzheng Co., LTD. TUNEL apoptosis detection kit, CHOPm and GRP78 monoclonal antibody, and CHOP and GRP78 immunohistochemistry kits were supplied by the Wuhan Boster Biotechnology Co., LTD.

Techniques: Flow Cytometry, Control, Saline

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:

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