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

Supplier: Proteintech

PRKAA2(protein kinase, AMP-activated, alpha 2 catalytic subunit), also named as AMPKA2, AMPK, PRKAA, AMPK2, belonogs to the CAMK Ser/Thr protein kinase family and SNF1 subfamily. PRKAA2 is an αβγ heterotrimer that is activated by low cellular energy status, such as decreases in both the ATP/AMP ratio and the phosphocreatine content and it is a glycogen synthase kinase, phosphorylating Ser7 at the NH2 terminus, which decreases glycogen synthase activity. The protein can be ubiquitinated.

Supplier: Bioss

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

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: Bioss

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

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: Bioss

Probable inhibitory regulator of the Ras-cyclic AMP pathway.

Supplier: Kewaunee

15 A electrical plugs for 48 or 72" benches.

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: Bioss

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

Supplier: Thermo Scientific Chemicals

Crystalline powder

Supplier: Ambeed

Fludarabine monophosphate 98%

Supplier: Boster Biological Technology

Rabbit IgG polyclonal antibody for Cyclic AMP-dependent transcription factor ATF-6 alpha(ATF6) detection. Tested with WB, IHC-P in Human;Mouse;Rat.

Supplier: Hach

Standard solution for accuracy checks in zinc determinations.

Supplier: Bioss

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq].

Supplier: Boster Biological Technology

Rabbit IgG polyclonal antibody for 5'-AMP-activated protein kinase subunit beta-1(PRKAB1) detection. Tested with WB in Human.

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: 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: 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.

Supplier: Bioss

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq].

Supplier: Bioss

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

Supplier: Promega Corporation

Recombinant full-length human AMPK (combination of A1/B1/G2 subunits) was expressed by baculovirus in Sf9 insect cells using a C-terminal His tag. AMP-activated protein kinase (AMPK) exhibits a key role as master regulator of cellular energy homeostasis.

Supplier: Clarity Diagnostics

Clarity CLIA Waived Drug Test Cup 10 Panel. Tests for the following: AMP, BAR, BZO, COC, MAMP (MET), MTD, OPI2000 (OPI), OXY, PCP, THC

Supplier: MP Biomedicals

Rifampin is a bactericidal antibiotic drug of the rifamycin group. It specifically inhibits DNA-dependent bacterial RNA Polymerase. Mammalian RNA polymerase is not affected.

Supplier: Hach

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

Supplier: Prosci

ADSSL1 is a muscle isozyme of adenylosuccinate synthase (EC 6.3.4.4), which catalyzes the initial reaction in the conversion of inosine monophosphate (IMP) to adenosine monophosphate (AMP).