recombinant human gdf8 Search Results


93
R&D Systems mouse recombinant myostatin
Fig. 3. <t>Myostatin</t> level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse <t>recombinant</t> myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.
Mouse Recombinant Myostatin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+gdf8/pm27965203-61-0-4?v=R%26D+Systems
Average 93 stars, based on 1 article reviews
mouse recombinant myostatin - by Bioz Stars, 2026-07
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93
R&D Systems r d systems 788 g8 010 activin
Fig. 3. <t>Myostatin</t> level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse <t>recombinant</t> myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.
R D Systems 788 G8 010 Activin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+gdf8/pmc05130356-118-168-168?v=R%26D+Systems
Average 93 stars, based on 1 article reviews
r d systems 788 g8 010 activin - by Bioz Stars, 2026-07
93/100 stars
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94
R&D Systems recombinant mouse gdf
Fig. 3. <t>Myostatin</t> level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse <t>recombinant</t> myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.
Recombinant Mouse Gdf, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+gdf8/pmc03148270-145-30-33?v=R%26D+Systems
Average 94 stars, based on 1 article reviews
recombinant mouse gdf - by Bioz Stars, 2026-07
94/100 stars
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93
R&D Systems gdf8 myostatin
Fig. 3. <t>Myostatin</t> level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse <t>recombinant</t> myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.
Gdf8 Myostatin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+gdf8/pmc11853584-267-4-30?v=R%26D+Systems
Average 93 stars, based on 1 article reviews
gdf8 myostatin - by Bioz Stars, 2026-07
93/100 stars
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N/A
The Recombinant Human GDF 8 Myostatin Protein from Novus Biologicals is derived from E coli The Recombinant Human GDF 8 Myostatin Protein has been validated for the following applications SDS Page
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N/A
The Recombinant Human Mouse Rat GDF 8 Myostatin Protein from R D Systems is derived from NS0 The Recombinant Human Mouse Rat GDF 8 Myostatin Protein has been validated for the following applications Bioactivity
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N/A
The Recombinant Human Mouse Rat GDF 8 Myostatin Protein from R D Systems is derived from NS0 The Recombinant Human Mouse Rat GDF 8 Myostatin Protein has been validated for the following applications Bioactivity
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N/A
Recombinant Human/Mouse/Rat GDF-8/Myostatin GMP Protein, CF
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N/A
The Recombinant Human Mouse Rat GDF 8 Myostatin GMP Protein from R D Systems is derived from NS0 The Recombinant Human Mouse Rat GDF 8 Myostatin GMP Protein has been validated for the following applications
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N/A
Human GDF-8 Recombinant Protein Tag Free Lyophilized from Innovative Research has been recombinantly produced in Human Cells. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of PBS,pH7.4. It is
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Image Search Results


Fig. 3. Myostatin level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse recombinant myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.

Journal: American journal of physiology. Endocrinology and metabolism

Article Title: Myostatin propeptide mutation of the hypermuscular Compact mice decreases the formation of myostatin and improves insulin sensitivity.

doi: 10.1152/ajpendo.00216.2016

Figure Lengend Snippet: Fig. 3. Myostatin level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse recombinant myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.

Article Snippet: Mouse recombinant myostatin (788-G8; R&D Systems) was used as a positive control.

Techniques: SDS Page, Recombinant, Positive Control, Knock-Out, Negative Control, Glycoproteomics

Fig. 5. Glucose tolerance and insulin sensitivity are improved by Compact myostatin mutation and reduced in congenic wild-type mice. Intraperitoneal (ip) glucose tolerance (A and B) and insulin sensitivity tests (C and D) of 3- to 4-mo-old (A and C) and 10-mo-old animals (B and D). Area under the curve (AUC) values are presented in bar diagrams. Data are reported as means SE. *P 0.05 and **P 0.01; n 3 Compact, 7 congenic wild-type, and 3 BALB/c mice (A), n 7 Compact, 3 congenic wild-type, and 6 BALB/c mice (B), n 3 Compact, 3 congenic wild-type, and 4 BALB/c mice (C), and n 6 Compact, 4 congenic wild-type, and 4 BALB/c mice (D).

Journal: American journal of physiology. Endocrinology and metabolism

Article Title: Myostatin propeptide mutation of the hypermuscular Compact mice decreases the formation of myostatin and improves insulin sensitivity.

doi: 10.1152/ajpendo.00216.2016

Figure Lengend Snippet: Fig. 5. Glucose tolerance and insulin sensitivity are improved by Compact myostatin mutation and reduced in congenic wild-type mice. Intraperitoneal (ip) glucose tolerance (A and B) and insulin sensitivity tests (C and D) of 3- to 4-mo-old (A and C) and 10-mo-old animals (B and D). Area under the curve (AUC) values are presented in bar diagrams. Data are reported as means SE. *P 0.05 and **P 0.01; n 3 Compact, 7 congenic wild-type, and 3 BALB/c mice (A), n 7 Compact, 3 congenic wild-type, and 6 BALB/c mice (B), n 3 Compact, 3 congenic wild-type, and 4 BALB/c mice (C), and n 6 Compact, 4 congenic wild-type, and 4 BALB/c mice (D).

Article Snippet: Mouse recombinant myostatin (788-G8; R&D Systems) was used as a positive control.

Techniques: Mutagenesis