9.4 proc traj macro software Search Results


crfk  (ATCC)
96
ATCC crfk
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Crfk, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 1 article reviews
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Shanghai Korain Biotech Co Ltd glucose regulated protein 94
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Glucose Regulated Protein 94, supplied by Shanghai Korain Biotech Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
Proteintech grp78 bip rabbit polyclonal antibody
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Grp78 Bip Rabbit Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Bio-Rad rabbit anti human grp94
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Rabbit Anti Human Grp94, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Boster Bio grp94
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Grp94, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews
grp94 - by Bioz Stars, 2026-07
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99
Danaher Inc goat polyclonal anti endoplasmin
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Goat Polyclonal Anti Endoplasmin, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Thermo Fisher gene exp hsp90b1 hs00427665 g1
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Gene Exp Hsp90b1 Hs00427665 G1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
ATCC zp 01385982 1 helicase recd traa
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Zp 01385982 1 Helicase Recd Traa, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Santa Cruz Biotechnology cells with endoplasmin grp94 sirna
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Cells With Endoplasmin Grp94 Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ATGen Inc hsp90b1 (grp94)
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Hsp90b1 (Grp94), supplied by ATGen Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
OriGene antibodies against hsp90b1
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
Antibodies Against Hsp90b1, supplied by OriGene, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Santa Cruz Biotechnology endoplasmin
( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection <t>in</t> <t>HEK293T</t> cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected <t>CRFK</t> cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .
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Image Search Results


( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection in HEK293T cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected CRFK cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .

Journal: Oncotarget

Article Title: A DNA telomerase vaccine for canine cancer immunotherapy

doi: 10.18632/oncotarget.26927

Figure Lengend Snippet: ( A ) Schematic maps and alignments of wild type cTERT and pDUV5 proteins. VDD: deletion in catalytic site at amino acid positions 858-860. NoLS, nucleolar localization signal; Ubi, ubiquitin; Flu, influenza A HLA-A2 restricted epitope; V5, V5 tag. ( B ) Expression of pDUV5 protein monitored 24 h post-transfection in HEK293T cells. Protein was detected using an anti-V5 mouse monoclonal antibody. pcDNA3.1 empty vector backbone as negative control. JP: jetPRIME. NT: non-treated cells. β-actin protein detection was used as a loading control assessment. ( C ) Intracellular localization of wild type hTERT and pDUV5 proteins in transfected QT6 cells visualized 24 h post-transfection with a rabbit anti-hTERT antibody or a mouse anti-V5 antibody respectively and a goat anti-rabbit-Alexa Fluor 488 conjugate or a goat anti-mouse antibody-Alexa Fluor 488 conjugate (green fluorescence) respectively. pcDNA3.1 vector as negative control. The nuclei were stained with DAPI (blue). The cells were analyzed for both fluorescence wavelengths (merged) upon fluorescence microscopy. ( D ) Neutralization of pDUV5 telomerase catalytic activity. Total cell proteins were extracted from wild type hTERT and pDUV5 transfected CRFK cells and telomerase activity was assessed by Telomeric Repeat Amplification Protocol (TRAP) assay. Relative Telomerase Activity (RTA; sample/positive control ratio) of pDUV5 compared to wild type hTERT and non-treated (NT) CRFK cells are displayed (n = 3 for 2.1 μg of total protein samples) using absorbance measurements values (OD450/690 nm). Mann-Whitney non-parametric test against non-treated CRFK cells, ** p < 0.01 .

Article Snippet: HEK293T (Human embryonic kidney) cell line and CRFK (Crandell-Rees feline kidney) cell line (from the ATCC) were cultured in Dulbecco’s Modified Eagle Medium (DMEM) supplemented with 10% heat-inactivated fetal calf serum (FCS), 1% sodium pyruvate, 1% penicillin/streptomycin pyruvate and 0.1% β-mercaptoethanol.

Techniques: Ubiquitin Proteomics, Expressing, Transfection, Plasmid Preparation, Negative Control, Control, Fluorescence, Staining, Microscopy, Neutralization, Activity Assay, Amplification, TRAP Assay, Positive Control, MANN-WHITNEY