Invitrogen

GAPDH Loading Control Monoclonal Antibody (GA1R), Alexa Fluor™ 555

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GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

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GAPDH Loading Control Antibody (MA5-15738-A555) in ICC/IF

Immunofluorescent analysis of GAPDH (red) in HeLa cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes and blocked with 3% Blocker BSA (Product # 37525) in PBS for 30 minutes at room temperature. Cells were stained with AlexaFluor 555 conjugated GAPDH monoclonal antibody (Product # MA5-15738-A555) at a dilution of 1:50 for 1 hour at ... View More

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

Product Image Gallery

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF) — Immunofluorescent analysis of GAPDH (red) in HeLa cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes and blocked with 3% Blocker BSA (Product # 37525) in PBS for 30 minutes at room temperature. Cells were stained with AlexaFluor 555 conjugated GAPDH monoclonal antibody (Product # MA5-15738-A555) at a dilution of 1:50 for 1 hour at room temperature. Nuclei (blue) were stained with Hoechst 33342 dye (Product # 62249). Images were taken on a Thermo Scientific ToxInsight at 20X magnification.

GAPDH Loading Control Antibody in Western Blot (WB) — Western blot analysis of GAPDH was performed by loading various cell lysates onto a 4-20% Tris-HCl polyacrylamide gel. Proteins were transferred to a low fluorescence PVDF membrane and blocked with Sea Block blocking buffer for at least 1 hour. The membrane was probed with a AlexaFluor555-conjugated GAPDH monoclonal antibody (Product # MA5-15738-A555) at a dilution of 1:500 for over night at 4C on a rocking platform and washed in TBS-0.1% Tween-20. Detection was performed using a fluorescence imaging system.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3 NGF prevents obesity- and diabetes-induced muscle atrophy through the Akt-dependent signaling pathway. ( a ) Representative immunoblots of p-Akt and Akt and densitometry of p-Akt/Akt ratio, * p < 0.05, Ln vs. HFS + STZ ( b ). ( c ) Representative immunoblots of the cytosolic fraction of p-FoxO1 and GAPDH and nuclear fraction of FoxO1 and Histone H3. ( d ) Densitometry of p-FoxO1 in cytosolic fraction. A significant decrease in phosphorylated FoxO1 is shown in HFS vs. Ln in the cytosolic fraction, * p < 0.05. ( e ) Densitometry of FoxO1 in nuclear fraction was significantly decreased in HFS + STZ + NGF vs. Ln+NGF, * p < 0.05. Data are shown as means +- SEM, n = 3 in each group. ( f ) FoxO1 translocation into the nucleus denoted by red arrows; FoxO1 is denoted by green arrows and nuclei is denoted by blue arrows; 40x; scale bar 20 mum; n = 3 in each group.

GAPDH Loading Control Antibody in Western Blot (WB) — FIGURE 6 Ad-KO mice have reduced ejection fraction, impaired cardiac function, increased autophagy and apoptosis after ischemia. (a) Representative western blot images of Beclin-1, LC3B, p62, and GAPDH from apex heart homogenates after MI. (b-d) Densitometry analysis of Beclin-1, LC3-II, and p62 to GAPDH from Figure 2a . (e) Representative TUNEL staining images in heart sections from WT and Ad-KO mice with or without ischemia surgery. (f) Quantification of TUNEL positive nuclei from Figure 3g . (g) Representative western blot images of BAX, Bcl2, Lcn2 (lipocalin 2), and GAPDH from apex hearts after MI. (h, i) Densitometry analysis of Bcl2 over BAX and Lcn2 over GAPDH. (j) Gross heart weight to tibial length ratio in WT and Ad-KO mice after 7 days MI. (k) Representative M-mode images of heart after MI. (l) Ejection fraction measured from 3B. (m) Representative images of B-mode showing changes in strains over three cardiac cycles in radial and longitudinal directions from hearts with or without ischemia surgery. (n, o) Quantification of average strains from six segments in Figure 3d . Results are presented as mean +- SEM ( n = 5 per group, biological replicates). * p < 0.05 versus corresponding sham. # p < 0.05 versus WT Ischemia. Two-way ANOVA with Bonferroni correction was run for statistical analysis. Scale bar = 50 mum. Ad-KO, adiponectin-knock out; ANOVA, analysis of variance; MI, myocardial infarction; WT, wild type.

GAPDH Loading Control Antibody in Western Blot (WB) — FIGURE 4 Accumulation of regional adiponectin at infarct zone after ischemia. (a) Representative western blot image of adiponectin and GAPDH in apex heart homogenates after 7 days (7D) MI. (b) Densitometry analysis of adiponectin over GAPDH in 1 day (1D) ischemia hearts. (c) Representative immunofluorescence images showing adiponectin (red) and WGA staining (green) in paraffin embedded heart after CAL. (d) Relative adiponectin mRNA expression over 18srRNA in heart apex after 7D MI. (e) ELISA quantification of adiponectin in serum after 1 day or 7 days MI. (f) Representative Western blot images of p-AMPK T172, p-ULK1 S555, and GAPDH in apex heart homogenates after 1D MI. (g-i) Densitometry analysis of adiponectin, p-AMPK T172 and p-ULK1 S555 to GAPDH from Figure 1f . Results are presented as mean +- SEM ( n = 5 per group for 7 days ischemia, n = 4 per group for 1 day ischemia, biological replicates). * p < 0.05 versus corresponding sham, # p < 0.05 versus WT MI. Two-way ANOVA with Bonferroni correction was performed in Figure 1g-i . Unpaired student t -test was run for statistical analysis in Figure 1b,d,e . Scale bar = 100 mum. Ad-KO, adiponectin-knock out; ANOVA, analysis of variance; CAL, coronary artery ligation; MI, myocardial infarction; ns, not significant; WGA, wheat germ agglutinin; WT, wild type.

GAPDH Loading Control Antibody in Western Blot (WB) — FIGURE 1 Adiponectin treatment enhanced autophagy flux in hypoxic cells in vitro. (a) DapRed fluorescence measured every hour in H9c2 cells during hypoxia or normoxia incubation with or without Ad (1 µg/mL). (b) DalGreen fluorescence measured every hour in H9c2 cells during hypoxia or normoxia incubation with or without Ad (1 µg/mL) for 24 h. (c) Representative Western blot images of p62, LC3 and GAPDH after hypoxia incubation with Ad for 12 h. (d, e) Densitometry analysis of p62 and LC3B-II to GAPDH from 5C. (f) Representative confocal microscope images of H9c2 cells stained with DalGreen and DapRed in normoxia or hypoxia conditions with or without Ad for 12 h. (g) Quantification of the green to red ratio from 5F. (h) Representative confocal microscope images of H9c2 cells stained with MagicRed after hypoxia incubation with Ad for 12 h. (i) Quantification of MagicRed fluorescence from 5H. Results are presented as mean +- SEM (n = 3 per group). * p < 0.05, ** p < 0.01, *** p < 0.001 versus control. Two-way ANOVA with Bonferroni correction was run for statistical analysis. Scale bar = 20 mum. Ad, adiponectin; ANOVA, analysis of variance; Con, control; Hypo, hypoxia; Nor, normoxia.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 9. Reduction of endogenous hnRNPK negatively impacts HTLV-1 IRES without affecting sHBZ IRES activity. HEK 293T cells were transfected with the dl DeltaEMCV, dl HTLV-1 IRES, or dl sHBZ IRES plasmids, proteins and RNAs were ultraviolet (UV) cross-linked (254 nm-irradiated with 400 mJ/cm 2 ). Endogenous hnRNPK was immunoprecipitated (IP) from cell extracts using protein A/G-agarose (PGA)-beads loaded with an anti-hnRNPK antibody or using PGA-beads loaded with an anti-IgG antibody as a negative control. ( A ) The hnRNPK protein present in the input extracts and the IPs were evaluated by western blotting using an anti-HA antibody. As a loading control, GAPDH was detected using an anti-GAPDH-specific antibody. The protein A/G HRP conjugated was used as the secondary antibody. ( B ) The quantity of FLuc encoding RNA (FLuc) or GAPDH encoding RNA (GAPDH) covalently bound to hnRNPK was determined by an RT-qPCR assay as described in (). RNA fold enrichment, as defined in (), obtained in the IP from cells transfected with the dl DeltaEMCV DNA, was set to 1. Values shown are the mean (+- SEM) from two independent experiments, with each RT-qPCR assay performed in duplicate. Statistical analyses were performed using the ANOVA Kruskal-Wallis test ( P < 0.05). ( C-H ) HEK293T cells were cotransfected with ( C- E ) the dl HTLV-1 IRES (200 ng), or ( F- H ) the dl sHBZ IRES (200 ng) plasmids, and a DscRNA (10 nM) control or DsiRNAK RNAs. Reduction of endogenous hnRNPK was monitored by

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 7. Inhibition of PRMT1 asymmetrical dimethylation impairs HIV-1 IRES activity. HEK 293T cells were cotransfected with the pNL-4.3-RLuc (200 ng) plasmid and 4 hpt treated, or not (only vehicle; (-)), with TC-E 5003 (0.125, 0.25, 0.50, 1 or 2 muM), a specific inhibitor of the PRMT1 activity. Total protein extracts were prepared 24 h post-treatment. ( A ) The PRMT1 activity (aDMA), and levels of the HIV-1 Gag-RLuc-HA fusion protein and endogenous hnRNPK in extracts from the untreated cell (lane 1) or from cells treated with at the different drug concentrations (0.125, 0.25, 0.50, 1 or 2 muM) were evaluated by western blot using GAPDH as a loading control. ( B ) RLuc activity was measured in proteins recovered from cells transfected with the pNL-4.3-RLuc plasmid and treated with 1 or 2 muM of TC-E-5003, and data are presented as RLA to the non-treated (-) cells set to 100%. Values shown are the mean (+- SEM) from three independent experiments, with each performed in duplicate. Statistical analysis was performed using ANOVA, followed by Dunnet's test (** P <= 0.01; ns, nonsignificant). ( C-E ) HEK293T cells were transfected with the dl HIV-1 IRES (200 ng) plasmid, and 4 hpt were treated, or not (only vehicle; (-)), with TC-E 5003 (1, or 2 muM). Total protein extracts were prepared 24 h post-treatment. ( C ) The PRMT1 activity (aDMA) and levels of endogenous hnRNPK in extracts from the untreated cell (lane 1) or from cells treated with 1 or 2 muM of TC-E 5003 were

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 6. hnRNPK post-translational modifications impact on HIV-1 IRES activity. HA-hnRNPK mutants (mut) for the phosphorylation or methylation sites were generated by site-directed mutagenesis of the HA-hnRNPK template plasmid (wt). HEK293T cells were cotransfected with the dl HIV-1 IRES (200 ng) together with each HA-hnRNPK (200 ng) plasmid (indicated in the X-axis). Total protein extracts were prepared 24 hpt. ( A ) Western blots were performed to detect the expression level of total hnRNPK and HA-hnRNPK proteins using GAPDH as a loading control. ( B ) Cell viability was determined by measuring the cellular metabolic activity using the MTS assay using dimethylsulfoxide (DMSO, 10%) as a control for cell death. Data are expressed relative to the viability of the cells transfected with control DNA (-) set to 100%. Values shown are the mean (+-SEM) from three independent experiments, with each performed in duplicate. Statistical analysis was performed using ANOVA, followed by Dunnet's test (*** P <= 0.001; ns = nonsignificant). ( C ) RLuc and FLuc activities were measured, and results are presented as RTA, relative to the activities in the presence of the HA-hnRNPK (wt), set to 100%. Values shown are the mean (+- SEM) from five independent experiments, with each performed in duplicate. Statistical analysis was performed using ANOVA, followed by Dunnet's test (* P <= 0.05; ** P <= 0.01; *** P <= 0.001; ns, nonsignificant). (D-F) H

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 5. Overexpression of hnRNPK does not enhance cryptic promoter activity of the dl HIV-1 DNA or induce alternative splicing of the dl HIV-1 IRES RNA. ( A ) HEK 293T cells were transfected with either the dl HIV-1 IRES (150 ng) or a promoterless DeltaSV40-dl HIV-1 IRES (150 ng) vector in the presence or the absence (-) of the HA-hnRNPK (100 ng) plasmid. 24 hpt total protein extracts were prepared. A schematic representation of the dl HIV-1 IRES and DeltaSV40-dl HIV-1 IRES plasmids is shown (upper panel). The expression of the HA-hnRNPK recombinant protein was determined by western blot, using the GAPDH protein as a loading control (middle panel). RLuc and FLuc activities were measured, and results are expressed as RLA relative to the activities obtained from the dl HIV-1 IRES vector when in the absence of the HA-hnRNPK, set to 100% (lower panel). Values shown are the mean (+-SEM) from three independent experiments, with each performed in duplicate. Statistical analysis was performed by an ordinary two-way ANOVA test (**** P < 0.0001; ns, nonsignificant). ( B ) The dl HIV-1 IRES (200 ng) was cotransfected with a control scRNA (50 nM) or with siRLuc (50 nM), in the presence or the absence (-), of the HA-hnRNPK (200 ng) plasmid. A schematic representation of the dl reporter targeted by the siRNA RLuc (siRLuc) targeting the Renilla luciferase ORF is shown (upper panel). Total protein extracts were prepared 48 hpt. The expression of the HA-hnRNPK was determi

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3. Reduction of endogenous hnRNPK levels in cells negatively impacts HIV-1 IRES activity. ( A ) Schematic representation of dl HIV-1 IRES mRNA. The capped and polyadenylated dual-luciferase (dl) bicistronic mRNA presents an upstream Renilla luciferase (RLuc) ORF and a downstream firefly luciferase (FLuc) ORF. A deleted 5'UTR of the encephalomyocarditis virus (DeltaEMCV) followed by the 5'UTR (nucleotides 1-336) of the HIV-1 vRNA, NL-4.3 clone, are placed between both cistrons. ( B-G ) HEK293T cells were cotransfected with the dl HIV-1 IRES (200 ng) mRNA encoding plasmid, a scRNA (200 nM), or a siRNAK ( B-D ) targeting hnRNPK or with a DscRNA (10 nM) control or DsiRNAK (E-G). Reduction of endogenous hnRNPK was monitored by western blot using GAPDH as a loading control ( B and E ). RLuc and FLuc activities were measured at 24 hpt, and data are presented as RLA ( C and F ) or as RTA ( D and G ). RTA corresponds to the FLuc/RLuc ratio that is used as an index of IRES activity. The RLA and RTA values obtained in the absence of HA-hnRNPK plasmid were set to 100%. ( H-J ) HEK293T cells were transfected with the dl HIV-1IRES plasmid with an irrelevant control DNA (200 ng) and DsiRNAK (10 mM) alone or with increasing concentrations (50-200 ng) of a plasmid encoding for a HA-hnRNPK. The levels of endogenous and overexpressed hnRNPKs were monitored by western blot ( H ). RLuc and FLuc activities were measured at 24 hpt, and data are presented as RLA ( I ) or as RTA ( J ). The RLA

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 4. Overexpression of hnRNPK promotes HIV-1 IRES activity. (A-D) HEK293T cells were cotransfected with the dl HIV-1 IRES (200 ng) and different quantities (50-200 ng) of a plasmid encoding for an HA-hnRNPK protein. ( A ) The presence of the endogenous hnRNPK and overexpressed HA-hnRNPK proteins was confirmed by western blot using GAPDH as a loading control. ( B ) Cell viability was determined by measuring the cellular metabolic activity using the MTS assay using dimethylsulfoxide (DMSO, 10%) as a control for cell death. Data are expressed relative to the viability of the cells transfected with control DNA (-) set to 100%. Values shown are the mean (+-SEM) from three independent experiments, with each performed in duplicate. Statistical analysis was performed by an ordinary one-way ANOVA test (*** P < 0.001). ( C, D ). RLuc and FLuc activities were measured at 24 hpt, and data are presented as RLA ( C ) or as RTA ( D ). The RLA and RTA values obtained in the absence of HA-hnRNPK plasmid were set to 100%. Values shown are the mean (+-SEM) from four independent experiments, with each performed in duplicate. Statistical analysis was performed using ANOVA, followed by Dunnet's test (* P <= 0.05; ** P <= 0.01; *** P <= 0.001; ns = nonsignificant). ( E ) Cytoplasmic RNA was extracted from cells transfected with dlHIV-1 IRES and pCMV3-HA-hnRNPK or with the control plasmid, pSP64-polyA. The relative amount of RNA was determined by

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 1. HnRNPK regulates HIV-1 Gag expression. ( A ) Schematic representation of the complete HIV-1 molecular clone pNL-4.3-RLuc. ( B ) HEK 293T cells were cotransfected with the pNL-4.3-RLuc (200 ng) plasmid and 10 nM of a DsiRNA targeting the hnRNPK mRNA (DsiRNAK) or with a scrambled RNA ((DscRNA); 10 nM) as a control. The expression of the HIV-1 Gag-RLuc-HA fusion protein and endogenous hnRNPK was determined 24 hpt by western blot using the GAPDH protein as a loading control. For the semi-quantitative comparative analysis, the captured images were quantified using the ImageJ 1.53 software (Windows version of NIH ImageJ, http://imagej.nih.gov/ij ). Values expressed in percentages (%) correspond to the ratio (OD value (p17 or hnRNPK) / OD value GAPDH) relative to the control (DscRNA) set to 100%. ( C ) Renilla luciferase activity was measured 24 hpt and is expressed as relative luciferase activity (RLA) relative to the activity obtained when the pNL-4.3-RLuc plasmid was cotransfected with the DscRNA(-) set to 100%. ( D ) Cytoplasmic RNA was extracted from cells expressing pNL-4.3-RLuc HIV-1 and treated with the DscRNA or the DsiRNAK (10 nM), and relative RNA levels were determined by real-time RT-qPCR. The RNA abundance was expressed relative to the value obtained for the cells treated with the DscRNA set to 100%. In ( C ) and ( D ), values represent the mean (+-SEM) from six independent experiments, with each conducted in duplicate. Statistical analyses were performed by

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 10. Overexpression of hnRNPK promotes the activity of the HTLV-1 IRES but not from the sHBZ IRES. HEK293T cells were cotransfected with ( A- C ) the dl HTLV-1 IRES (200 ng), or ( D-F ) or the dl sHBZ IRES (200 ng) plasmids, and the HA-hnRNPK encoding plasmid. The presence of the overexpressed HA-hnRNPK protein was confirmed by western blot using GAPDH as a loading control ( A and D ). RLuc and FLuc activities were measured at 24 hpt, and data are presented as RLA ( B and E ) or RTA ( C and F ). The RLA and RTA values obtained in the absence of HA-hnRNPK plasmid were set to 100%. Values represent the mean (+- SEM) from three independent experiments, each conducted in duplicate. Statistical analysis was performed by ANOVA (* P < 0.05).

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 6 ATF6 is processed during L. pneumophila infection. ( a ) RAW 264.7 cells were left uninfected or infected with either WT L. pneumophila , DeltadotA , B. Delta5, Delta5+plgt2, or Delta5 plgt2* (catalytically dead lgt2) at an MOI of 150. Cells were then left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) for 6 h. Full-length ATF6 (pATF6) and cleaved pATF6(N) were monitored via immunoblot. Full blots for Fig. 6a are provided in Supplementary Fig. 5 . ( b ) HEK-293 FCgamma cells infected with either WT L. pneumophila or DeltadotA and then treated for 6 h with Tg (1 mug mul -1 ). Sel1L mRNA levels were then monitored via qRT-PCR, with GAPDH serving as an endogenous control. Two biological replicates were used each with three technical replicates using the identical experimental conditions. Values in all graphs are means+-s.e.m. * P <0.05; Student's t -test. ( c ) Cleaved and uncleaved ATF6 levels were similarly monitored in cells treated with CHX; 1 mug mul -1 ), Tg (1 mug mul -1 ), Tg and CHX, or left untreated for 6 h. Full blots for Fig. 6b are provided in Supplementary Fig. 5 . ( d ) RAW267.4 cells were infected with either WT L. pneumophila or the DeltadotA strain at an MOI of 150 and cells were then treated with Tg (1 mug mul -1 ) or left untreated for 6 h. ATF6 mRNA transcript levels were monitored via qRT-PCR. Two biological replicates were used each with three technical replicates using the identical experimental conditions. Values in all graphs

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3 Suppression of ER stress is an effector driven process that is independent of the mTOR pathway. ( a - c ) HEK-293 FCgamma cells were either left uninfected or infected with WT L. pneumophila or DeltadotA L. pneumophila at an MOI of 150. Cells were then either left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) or treated with a combination of Tg and the antibiotic Rifampicin (Rif.; 2 mug mul -1 ) for 6 h. After 6 h phase contrast images were taken. ( d ) HEK-293 FCgamma cells were infected at an MOI of 150 with WT L. pneumophila , or left uninfected. Cells were then treated with Rif. alone (2 mug mul -1 ), Rif. with Tg (1 mug mul -1 ), Tg (1 mug mul -1 ) alone or left untreated for 6 h. BiP protein levels were monitored via immunoblot. ( e ) HEK-293 FCgamma cells were untreated or treated with rapamycin (10 nM) or rapamycin with Tg (1 mug mul -1 ) for 6 h. BiP protein levels were then monitored via immunoblot and levels of phosphorylated Akt at serine 473 (P-Akt) were monitored from these lysates via immunoblot. ( f ) RAW 264.7 cells were infected with WT L. pneumophila, dotA , or Delta 5 strains of L. pneumophila at an MOI of 150. BiP protein expression was monitored via immunoblot. GAPDH was used as a loading control. Full blots for Fig. 3d-f are provided in Supplementary Fig. 5 .

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 1 Expression of two critical components of the UPR, BiP and CHOP are blocked by L. pneumophila ( a ) Caspase 1/11 (-/-) bone marrow derived macrophages or ( b ) HEK-293 FCgamma cells-expressing Fc gamma (HEK-293 FCgamma) were either left uninfected or infected with WT or DeltadotA strains of L. pneumophila at an MOI of 150. Cells were then left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) for 6 h. BiP, CHOP and PDI protein expression were monitored via immunoblot. GAPDH was used as a loading control. Full blots are provided for Fig. 1a,b in Supplementary Fig. 5 . ( c , d ) BiP and CHOP levels were quantified respectively from three biological replicates using the same experimental conditions in HEK-293 FCgamma cells. Data are depicted as the fold change normalized to uninfected levels. Data represent three independent experiments. Values in all graphs are means+-s.e.m. * P <0.05; Student's t -test.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 6. The N-tails of H2A and H3 are epistatic to RAD18 . ( A ) Epistasis studies of (i) N-tail deletion mutants combinatorially deleted for (ii) MAG1 , (iii) REV3 , (iv) RAD5 and (v) RAD18 . ( B ) Epistasis study of N-tail deletion mutants combinatorially deleted for RAD52 . ( C ) MMS survival assay of WT and N-tail mutants (solid lines) and the N-tail mutants combinatorially deleted for RAD18 (dashed lines). ( D ) Growth curves of the cells in ( C ) in the absence of MMS. ( E ) Western blot of PCNA 9myc in WT and N-tail mutants before UV exposure and after a 1 h recovery in YPD following 100 J/m 2 of UV irradiation. GAPDH is used as the loading control. rad6Delta serves as a negative control for PCNA ubiquitylation. ( F ) Quantifications of (E) by normalizing (PCNA 9myc -ub)/(PCNA 9myc -total) and (PCNA 9myc -ub 2 )/(PCNA 9myc -total) to WT. Error bars indicate standard deviations from three independent experiments.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3. Mag1 protein expression and MAG1 mRNA expression are reduced in tH2A:tH3 cells. WT and the N-tail deletion mutants were treated with 0.2% MMS for 10 min and further analyzed at the indicated time points. ( A ) Mag1 9myc and GAPDH were detected via western blotting. ( B ) A northern blot detecting MAG1 and reprobed for RDN18 . [We note that the small band shift between the tH3(60') sample and the tH2A:tH3 samples is due to a gel running artifact]. ( C ) Quantification of different gels, such as shown in (B) by normalizing MAG1 levels to that of WT in the absence of MMS. Error bars indicate standard deviations derived from three independent experiments.

产品信息

MA5-15738-A555

应用

建议稀释比

已发表文章

免疫印迹 (WB)

1:500

查看7篇已发表文章 7篇已发表文章

免疫细胞化学 (ICC/IF)

1:25-1:100

-

产品规格

种属反应

Bacteria, Chicken, Hamster, Human, Insect, Mouse, Rabbit, Rat, Yeast

已发表种属

Human

宿主/亚型

Mouse / IgG1

分类

Monoclonal

类型

Antibody

克隆号

GA1R

抗原

recombinant GAPDH

偶联物

Alexa Fluor™ 555 Alexa Fluor™ 555 Alexa Fluor™ 555

激发/发射光谱

553/568 nm 查看光谱

形式

Liquid

浓度

1 mg/mL

纯化类型

Protein A

保存液

PBS with 1mg/mL BSA

内含物

0.05% sodium azide

保存条件

4°C, do not freeze

运输条件

Ambient (domestic); Wet ice (international)

AB_2609744

靶标信息

GAPDH (Glyceraldehyde-3-phosphate dehydrogenase) is a catalytic enzyme commonly known to be involved in glycolysis. GAPDH exists as a tetramer of identical 37-kDa subunits and catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, GAPDH is ubiquitously expressed and displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication, DNA repair, nuclear RNA export, membrane fusion and microtubule bundling. Studies provide evidence of GAPDH playing an essential part in gene expression observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases. Further, GAPDH is involved in other cellular processes ranging from membrane fusion, and neuronal apoptosis in cancer. GAPDH is reported to bind to a variety of other proteins, including the amyloid precursor protein, mutations in which cause some forms of Alzheimer's disease (AD), and the polyglutamine tracts of Huntingtin, the protein product aberrant forms of which are causative of Huntington's disease. Associations between GAPDH, actin and tubulin have also be reported. Since GAPDH is expressed at high levels in most tissues, it is useful as protein loading control in Western Blot analysis.

仅用于科研。不用于诊断过程。未经明确授权不得转售。

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Ortiz DA,Glassbrook JE,Pellett PE

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

Thu Sep 01 00:00:00 UTC 2016

The amino-terminal tails of histones H2A and H3 coordinate efficient base excision repair, DNA damage signaling and postreplication repair in Saccharomyces cerevisiae.

Nucleic acids research

Meas R,Smerdon MJ,Wyrick JJ

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

Tue May 26 00:00:00 UTC 2015

Legionella suppresses the host unfolded protein response via multiple mechanisms.

Nature communications

Treacy-Abarca S,Mukherjee S

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A555) in Western Blot

Wed Jul 29 00:00:00 UTC 2015

生物信息学

蛋白别名: 38 kDa BFA-dependent ADP-ribosylation substrate; aging-associated gene 9 protein; BARS-38; EC 1.2.1.12; epididymis secretory protein Li 278; epididymis secretory sperm binding protein Li 162eP; GAPDH; GAPDH-2; glceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase type 2; glyceraldehyde-3-phosphate dehydrogenase, spermatogenic; Glyceraldehyde-3-phosphate dehydrogenase, testis-specific; HGNC:4141; MGC88685; multifunctional protein, glycolytic enzyme; Peptidyl-cysteine S-nitrosylase GAPDH; Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2; Spermatogenic glyceraldehyde-3-phosphate dehydrogenase; unnamed protein product

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基因别名: BARS-38; CDABP0047; G3PD; GAPD; Gapd-s; GAPD2; GAPDH; GAPDH-2; GAPDH2; GAPDHS; GAPDS; HEL-S-162eP; HEL-S-278; HSD-35; HSD35; I79_001391; KNC-NDS6; OK/SW-cl.12

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UniProt ID: (Rabbit) P46406, (Human) P04406, (Chicken) P00356, (Human) O14556, (Mouse) P16858, (Chinese hamster) P17244, (Rat) P04797, (Rat) Q9ESV6, (Mouse) Q64467

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Entrez Gene ID: (Rabbit) 100009074, (Human) 2597, (Chicken) 374193, (Human) 26330, (Rabbit) 100352213, (Mouse) 14433, (Chinese hamster) 100736557, (Rat) 24383, (Rat) 66020, (Mouse) 14447, (Chinese hamster) 100767862

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glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity protein binding microtubule binding peptidyl-cysteine S-nitrosylase activity identical protein binding NADP binding NAD binding aspartic-type endopeptidase inhibitor activity disordered domain specific binding molecular_function oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor dehydrogenase

microtubule cytoskeleton organization gluconeogenesis regulation of macroautophagy negative regulation of translation peptidyl-cysteine S-trans-nitrosylation protein stabilization neuron apoptotic process canonical glycolysis cellular response to interferon-gamma nuclear membrane fusion glycolytic process negative regulation of endopeptidase activity negative regulation of apoptotic process positive regulation of cytokine secretion defense response to fungus killing by host of symbiont cells positive regulation by organism of apoptotic process in other organism involved in symbiotic interaction oxidation-reduction process antimicrobial humoral immune response mediated by antimicrobial peptide spermatid development sperm motility positive regulation of glycolytic process carbohydrate metabolic process apoptotic process multicellular organism development response to ammonium ion regulation of translation glucose metabolic process