human skeletal muscle Search Results


muscle cell basal medium cell applications  (Cell Applications Inc)
96
Cell Applications Inc muscle cell basal medium cell applications
Muscle Cell Basal Medium Cell Applications, supplied by Cell Applications Inc, 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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human skeletal muscle  (TaKaRa)
94
TaKaRa human skeletal muscle
Human Skeletal Muscle, supplied by TaKaRa, 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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primary human skeletal derived myoblasts  (Cook MyoSite Inc)
94
Cook MyoSite Inc primary human skeletal derived myoblasts
Primary Human Skeletal Derived Myoblasts, supplied by Cook MyoSite Inc, 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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skmc media  (PromoCell)
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PromoCell skmc media
Skmc Media, supplied by PromoCell, 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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marathon ready skeletal muscle cdna  (TaKaRa)
94
TaKaRa marathon ready skeletal muscle cdna
Marathon Ready Skeletal Muscle Cdna, supplied by TaKaRa, 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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human skeletal muscle cell differentiation medium  (Cell Applications Inc)
92
Cell Applications Inc human skeletal muscle cell differentiation medium
Human Skeletal Muscle Cell Differentiation Medium, supplied by Cell Applications Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human skm cdna library for yth  (TaKaRa)
95
TaKaRa human skm cdna library for yth
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Human Skm Cdna Library For Yth, supplied by TaKaRa, 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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skeletal muscle polya rna  (TaKaRa)
94
TaKaRa skeletal muscle polya rna
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Skeletal Muscle Polya Rna, supplied by TaKaRa, 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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skeletal muscle growth medium cat  (Cell Applications Inc)
93
Cell Applications Inc skeletal muscle growth medium cat
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Skeletal Muscle Growth Medium Cat, supplied by Cell Applications Inc, 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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human myoblasts  (PromoCell)
93
PromoCell human myoblasts
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Human Myoblasts, supplied by PromoCell, 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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human peripheral nerve cells  (Innoprot Inc)
90
Innoprot Inc human peripheral nerve cells
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Human Peripheral Nerve Cells, supplied by Innoprot 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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human skeletal muscle  (Santa Cruz Biotechnology)
88
Santa Cruz Biotechnology human skeletal muscle
The N-terminal region of PLEIAD interacts with CTBP1. (a) <t>YTH</t> screening using a human <t>skm</t> <t>cDNA</t> library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).
Human Skeletal Muscle, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


The N-terminal region of PLEIAD interacts with CTBP1. (a) YTH screening using a human skm cDNA library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).

Journal: Journal of molecular biology

Article Title: PLEIAD/SIMC1/C5orf25, a Novel Autolysis Regulator for a Skeletal-Muscle-Specific Calpain, CAPN3, Scaffolds a CAPN3 Substrate, CTBP1

doi: 10.1016/j.jmb.2013.05.009

Figure Lengend Snippet: The N-terminal region of PLEIAD interacts with CTBP1. (a) YTH screening using a human skm cDNA library identified CTBP1 as a binding protein for PLEIAD. The functional annotation for human CTBP1 is shown. Among previously validated missense mutants, four different mutants that compromised complex formation activities of CTBP1 were selected. The mouse sequence has an insertion of 1 aa at the C-terminal region and therefore consists of 441 aa. Horizontal bar indicates the antigenic polypeptides for anti-CTBP1. (b) The N-terminal region, hPLEIAD-N or hPLEIADf: ex4term, was sufficient for the interaction (3D and 4D), while the C-terminal region, hPLEIAD-C, shared by both hPLEIADa and f, failed to undergo detectable interaction (5D). Two different mutations in PXDLS-binding domain of CTB1 showed negative effect on its interaction with PLEIAD (2F to 4F and 2H to 4H). (c) Complex formation of CAPN3, PLEIAD, and CTBP1 was examined using wheat-germ cell-free expression system. In addition to the layer of mRNA and other components for translation reaction, solution of CTBP1 protein was set on the bottom of the tube. After translation, layers were mixed and subjected to immunoprecipitation using anti-CAPN3 antibody. (d) Both PLEIADa and PLEIADf were coimmunoprecipitated with CAPN3:CS (lanes 5 and 7, CBB and anti-His). In these samples, CTBP1 was also detected (anti-CTBP1). Numbers in parentheses indicate the percentage of the total amount. Nonspecific degradation or precipitation of CTBP1 during translation reaction was not detected (data not shown).

Article Snippet: The human skm cDNA library for YTH (Clontech) or mouse skm cDNA synthesized from total RNA was used as a template.

Techniques: cDNA Library Assay, Binding Assay, Functional Assay, Sequencing, Expressing, Immunoprecipitation