1811 Results for: "gradues&amp"

Supplier: Boster Bio

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

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

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

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

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: Boster Bio

Rabbit IgG polyclonal antibody for 5'-AMP-activated protein kinase subunit beta-2(PRKAB2) detection. Tested with WB, IHC-P in Human;Mouse;Rat.

Supplier: Boster Bio

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: ProSci Inc.

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).

Supplier: ProSci Inc.

FUNCTION: Produces green light with a wavelength of 562 nM.
CATALYTIC ACTIVITY: Photinus luciferin + O₂ + ATP = oxidized Photinus luciferin + CO₂ + AMP + diphosphate + light.
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
COFACTOR: Magnesium.
SUBCELLULAR LOCATION: Peroxisomal.

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

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: Abcam

Potent, selective, reversible AMP-kinase inhibitor. BMP type I receptor inhibitor. 1 * 10 mg

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.

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: MP Biomedicals

PGI2 is synthesized primarily in vascular endothelial cells. It is a potent inhibitor of platelet aggregation, relaxes vascular smooth muscle, and also increases cyclic AMP concentration in human platelets.

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.

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. [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. [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. [provided by RefSeq, Jul 2008].