3335 Results for: "PINNACLE+BRUSH&amp"

Supplier: ENZO LIFE SCIENCES

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

Supplier: Restek

Pinnacle® DB PFP Propyl, a unique pentafluorophenyl phase with a propyl spacer, uses a highly base-deactivated spherical silica manufactured by Restek. This highly base-deactivated packing exhibits excellent peak shapes for a wide range of compounds, including nucleosides, nucleotides and halogenated compounds.

Supplier: Avantor Fluid Handling

Quickly and easily replace components of your Masterflex system.

Supplier: ENZO LIFE SCIENCES

PKA activator.

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: 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: Thermo Fisher Scientific

Bright brushing gold.

Supplier: LIOFILCHEM

Multodisc with eight antimicrobial agents on a ring.

Supplier: Apollo Scientific

Adenosine 5'-monophosphate disodium salt (from yeast)

Supplier: Restek

Base-deactivated spherical silica that is optimised for UHPLC stability. Designed to resolve complex mixtures of polycyclic aromatic hydrocarbons (PAHs). Complete resolution of all 16 EPA 610 PAHs, plus two other routinely analyzed PAH compounds, in less than five minutes to greatly reduce run times and increase sample throughput.

Supplier: NASCO FORT ATKINSON

Accessory for fluid samplers, Cleaning brush for Sludge Judge and Sludge Judge Ultra, 183 cm

Supplier: VWR Collection

Cleaning kit containing a puffer brush (lens cleaning brush), cotton cloth and pair of nitrile gloves.

Supplier: Apollo Scientific

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

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: Avantor Fluid Handling

Operate a 230-240 VAC motor with only a 115 VAC power supply.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Brady

This fuse lockout device has been designed to prevent the unintended re-energisation of an energy source through a fuse. The device fits most fuse holders between 20 Amps and 400 Amps.

Supplier: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

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/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: WATER ID PRIMELAB

Multiparameter colorimeter, Cleaning brush

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

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: 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.