39854 Results for: "Füllkörper für Destilliersäulen&amp"

Supplier: US Biological

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

Supplier: ENZO LIFE SCIENCES

Competitive inhibitor of cyclic AMP-dependent protein kinase I and II.Metabolic stability towards mammalian cyclic nucleotide- responsive phosphodiesterases.
Discriminates between protein kinase A (antagonist) and some other cyclic AMP receptors, e.g. channels or CAP 3 (agonist).Membrane-permeant for several systems (for improved permeability more lipophilic analogues e.g. Rp-8-Br-cAMPS are recommended).

Supplier: LIOFILCHEM

Multodisc with eight antimicrobial agents on a ring.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

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: 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: US Biological

Anti-cyclic AMP Rabbit Polyclonal Antibody

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: SURESCREEN

These multipanel drugs tests can detect up to 12 drugs simultaneously.

Supplier: Bioss

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities.

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 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: SURESCREEN

AMP/BZO/BUP/COC/MTD/OPI six parameter multi-panel dip urine drug testdrug test with parameter.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Apollo Scientific

Rifampicin is active against gram-positive but less active against gram-negative bacteria.

Supplier: Bioss

Adenylsuccinate lyase is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. It catalyzes two reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to give aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to give AMP. Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and , in some cases, growth retardation associated with muscle wasting and epilepsy. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Adenylsuccinate lyase is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. It catalyzes two reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to give aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to give AMP. Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and , in some cases, growth retardation associated with muscle wasting and epilepsy. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: US Biological

Anti-AMP Activated Protein Kinase alpha1/AMPKa2 Rabbit Polyclonal Antibody