105899 Results for: "Biotin-PEG6-Acid&amp"

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localised to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.