11057 Results for: "Trimellitic anhydride chloride&amp"

Supplier: US Biological

Anti-Cyclic AMP Rabbit Polyclonal Antibody

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: PanReac AppliChem

Rifampicin

Supplier: Apollo Scientific

Adenosine 5'-monophosphate disodium salt (from yeast)

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

The protein encoded by this gene can hydrolyse substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester, and AMP-NH2. The encoded protein interacts with these substrates via a histidine triad motif, which is part of the loop that binds to the substrate. This gene has been found to be a tumour suppressing gene. Several transcript variants, but only one of them protein-coding, have been found for this gene.

Supplier: Bioss

The protein encoded by this gene can hydrolyze substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester, and AMP-NH2. The encoded protein interacts with these substrates via a histidine triad motif, which is part of the loop that binds to the substrate. This gene has been found to be a tumor suppressing gene. Several transcript variants, but only one of them protein-coding, have been found for this gene. [provided by RefSeq, Dec 2012].

Supplier: Bioss

The protein encoded by this gene can hydrolyze substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester, and AMP-NH2. The encoded protein interacts with these substrates via a histidine triad motif, which is part of the loop that binds to the substrate. This gene has been found to be a tumor suppressing gene. Several transcript variants, but only one of them protein-coding, have been found for this gene. [provided by RefSeq, Dec 2012].

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Merck

Trifluoroacetic anhydride, Supelco®

Supplier: US Biological

Anti-Cyclic AMP Dependent Protein Kinase Regulatory Subunit 1b Sheep Polyclonal Antibody

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism. Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterised by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

The protein encoded by this gene can hydrolyze substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester, and AMP-NH2. The encoded protein interacts with these substrates via a histidine triad motif, which is part of the loop that binds to the substrate. This gene has been found to be a tumor suppressing gene. Several transcript variants, but only one of them protein-coding, have been found for this gene. [provided by RefSeq, Dec 2012].

Supplier: TCI

Adenosine-3',5'-cyclic monophosphate sodium salt ≥98.0% (by HPLC)

Supplier: LIOFILCHEM

Multodisc with eight antimicrobial agents on a ring.

Supplier: Bioss

AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.

Supplier: Bioss

AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.

Supplier: Merck

Trifluoromethanesulphonic anhydride for synthesis, Sigma-Aldrich®

Supplier: TCI

Rifampicin ≥98.0% (by titrimetric analysis)

Supplier: SIGMA ALDRICH MICROSCOPY

2-Sulphobenzoic cyclic anhydride ≥90%, Sigma-Aldrich®

Supplier: Merck

Pentafluoropropionic anhydride ≥99% for GC derivatisation, Supelco®

Supplier: Merck

1,2,3,6-Tetrahydrophthalic anhydride, Sigma-Aldrich®

Supplier: Merck

Trifluoroacetic anhydride ≥99% (by GC) for synthesis

Supplier: Merck

Dodecenylsuccinic anhydride (mixture of isomers), Sigma-Aldrich®

Supplier: Merck

2-Sulphobenzoic cyclic anhydride for synthesis, Sigma-Aldrich®

Supplier: ENZO LIFE SCIENCES

Cell-permeable, potent and AMP-competitive inhibitor of glycogen phosphorylase.