57051 Results for: "2-Amino-9-fluorenone&amp"

Supplier: Thermo Fisher Scientific

2-Amino-9-fluorenone 98%

Supplier: VWR Chemicals

5% water has been added to maintain liquidity at room temperature.

Supplier: Merck

AMP (2-Amino-2-methylpropanol) for synthesis, Sigma-Aldrich®

Supplier: Merck

1-Amino-9-fluorenone, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol), (max. 5% H₂O) 95%

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol) 99%

Supplier: Apollo Scientific

Used for the preparation of buffer solutions, suitable for the determination of alkaline phosphatase.

Supplier: Thermo Fisher Scientific

Adenosine-5'-monophosphoric acid (AMP) 99%

Supplier: Merck

9-Fluorenone for synthesis, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific

a useful ligand determinant that facilitate the binding of APS reductase inhibitors and activates adenosine receptor agonists.

Supplier: ENZO LIFE SCIENCES

Adenosine 5'-monophosphate disodium salt (AMP disodium salt) ≥98% (by HPLC)

Supplier: Apollo Scientific

Adenosine 5'-monophosphate monohydrate ≥96%

Supplier: Thermo Fisher Scientific

9-Fluorenone ≥98%

Supplier: Thermo Fisher Scientific

9-Fluorenone 99+%

Supplier: Apollo Scientific

4-Aza-9-fluorenone

Supplier: Apollo Scientific

2-Fluoro-9-fluorenone 98%

Supplier: Merck

2-Acrylamido-2-methylpropanesulphonic acid for synthesis, Sigma-Aldrich®

Supplier: ENZO LIFE SCIENCES

PKA activator.

Supplier: Apollo Scientific

2-Bromo-9-fluorenone

Supplier: Apollo Scientific

Adenosine-3',5'-cyclic monophosphate (cAMP) 97%

Supplier: Thermo Fisher Scientific

3,6-Di-tert-butyl-9-fluorenone ≥99%

Supplier: Thermo Fisher Scientific

2-Hydroxy-9-fluorenone ≥97%

Supplier: Thermo Fisher Scientific

Adenosine-3',5'-cyclic monophosphate (cAMP) 99+%

Supplier: Thermo Fisher Scientific

9-Fluorenone oxime ≥98%

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.