63666 Results for: "sample+filtration+&amp"

Supplier: Prosci

NUDT9 hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.

Supplier: FOUR E’S INDUSTRIAL GROUP INC.

Omolality calibration standards for clinical and research osmometers.

Supplier: Boster Biological Technology

Rabbit IgG polyclonal antibody for Cyclic AMP-dependent transcription factor ATF-4(ATF4) detection. Tested with WB in Human.

Supplier: Bachem Americas

Specific substrate for the sucrose-non-fermenting protein kinase (SNF1) from Saccharomyces cerevisiae and its mammalian counterpart, AMP-activated protein kinase (AMPK).

Supplier: Kewaunee

15 A electrical plugs for 48 or 72" benches.

Supplier: Bioss

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

Supplier: Bioss

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

Supplier: Proteintech

AMPD1, also named as MAD and MADA, belongs to the adenosine and AMP deaminases family. AMP deaminase plays a critical role in energy metabolism. It catalyzes the reaction: AMP + H2O = IMP + NH3. Defects in AMPD1 are the cause of adenosine monophosphate deaminase deficiency muscle type (AMPDDM) which is a metabolic disorder resulting in exercise-related myopathy. The antibody is specific to AMPD1.

Supplier: Bachem Americas

AIP, non-phosphorylatable analog of autocamtide-2 (H-3218), was found to be a highly specific and potent inhibitor of calmodulin-dependent protein Kinase II (IC₅₀= 40 nM) without affecting cyclic AMP-dependent protein kinase, protein kinase C and calmodulin-dependent protein kinase IV.

Supplier: Hach

Acetate standard solution for accuracy checks in volatile acids determinations.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.

Supplier: Bioss

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

Supplier: Bioss

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

Supplier: Cayman Chemical Company

Cyclic di-nucleotide phosphodiesterase (CdnP, also known as Rv2837c) is a soluble, stand-alone phosphodiesterase in regulating cyclic dinucleotide signaling during intracellular infections of M. tuberculosis{36095}. Studies have found that CdnP is capable of hydrolyzing cyclic di-adenosine monophosphate (c-di-AMP; Item No. 17753) into two AMPs as a strategy to avoid activation of the innate immune response of the host. M. tuberculosis infection leads to cytosolic release of c-di-AMP, which is recognized by stimulator of interferon genes (STING) and subsequently triggers type I interferon response. Other studies have shown that deletion or inhibition of CdnP attenuates the M. tuberculosis virulence both in vitro and in vivo.

Supplier: Thermo Scientific Chemicals

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

Supplier: Hach

Standard solutions for accuracy checks in nitrate nitrogen determinations and also for meter calibrations/standardisation.

Supplier: Bioss

Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.

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: Alere

Rapid Drug Screen for the simultaneous, qualitative detection of single or multiple drug metabolites in human urine

Supplier: Alere

Rapid Drug Screen for the simultaneous, qualitative detection of single or multiple drug metabolites in human urine

Supplier: Genetex

Rabbit Polyclonal antibody to DAK (bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing))

Supplier: ALADDIN SCIENTIFIC

Acadesine results in accumulation of ZMP, which mimics the stimulating effect of AMP on AMPK and AMPK kinase.An inhibitor of the transcription of PPARα, the coactivation of PPARα.

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: 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: WALLCUR, LLC.

Prefilled And Etched For Proper Breakage.

Supplier: CLOUD-CLONE CORP MS

Polyclonal Antibody to Protein Kinase, AMP Activated Alpha 1 (AMPK Alpha 1), derived from recombinant AMPK Alpha 1(Ile28~Lys257), is reactive with Human/Mouse.

Supplier: Hach

Standard solution for accuracy checks in zinc determinations.