146018 Results for: "3-Hydroxypropanesulfonic+acid&amp"

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interacts with G proteins (heterotrimeric GTPases) to synthesize intracellular second messengers such as diacylglycerol, cyclic AMP, inositol phosphates and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling, along with involvement in many pathological conditions. GPR31 (G-protein coupled receptor 31) is a 319 amino acid orphan receptor that localizes to the cell membrane. GPR31 shares 25-33% homology with members of the chemokine, purino and somatostatin receptor gene families.

Supplier: MP Biomedicals

CHAPSO is the hydroxy analog of CHAPS; a non-denaturing zwitterionic detergent for solubilizing proteins, especially integral membrane proteins while maintaining the functional capability of the protein of interest.

Supplier: Proteintech

AARS2(Alanine--tRNA ligase, mitochondrial) is also named as KIAA1270, AARSL, bA444E17.1, AlaRS, AARSL, COXPD8, MTALARS, MT-ALARS and belongs to the class-II aminoacyl-tRNA synthetase family. It catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). It also edits incorrectly charged tRNA(Ala) via its editing domain. The full length 107 kDa protein has a transit peptide with 23 amino acids.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: RPI

(3-((3-Cholamidopropyl)dimethylammonio)-2-hydroxy-1-propanesulfonate)

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Matrix Scientific

Matrix Scientific Part Number: 058419-500MG , MDL Number: MFCD00038350

Supplier: VWR

5% water has been added to maintain liquidity at room temperature.

Supplier: Prosci

The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

Supplier: Rockland Immunochemical

PAPOLA is an RNA polymerase that generates the poly(A) tail of RNA’s by adding AMP monomers to the 3’-end. PAPOLA may also be required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. Anti-PAPOLA Antibody is ideal for research in Gene Expression, Transcription and Translation.

Supplier: Genetex

One of the many phosphodiesterases that compartmentalize and hydrolyze cAMP and cGMP into AMP and GMP is Phosphodiesterase type 11. The human PDE11A contains an open reading frame encoding a 490 amino acid protein (55-56 kDa). The PDE11A has an N-terminus GAF domain homologous to other signaling molecule as found in PDE2, PDE5, PDE6, PDE10, which potentially represents an allosteric cGMP and other small signaling molecules. PDE11A hydrolyzes both cGMP and cAMP; it is sensitive to non-selective PDE inhibitor IBMX as well as zaprinast and dipyrimadole inhibitors that are generally selective for cGMP-specific enzymes. PDE11A expression is diverse and is found in high levels in skeletal muscle, prostate, kidney, liver, pituitary and testis.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Prosci

For WB starting dilution is: 1:1000

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Prosci

For WB starting dilution is: 1:1000

Supplier: Prosci

For WB starting dilution is: 1:1000

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Prosci

For WB starting dilution is: 1:8000

Supplier: Bioss

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008].

Supplier: Bioss

G protein-coupled receptors (GPCRs) represent a large superfamily of cell-surface receptors that are involved in a multitude of physiological processes such as perception of sensory information, modulation of synaptic transmission, hormone release/actions, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesize intracellular second messengers, such as diacylglycerol, cyclic AMP, inositol phosphates and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling and are involved in many pathological conditions. GRIN2 (G protein-regulated inducer of neurite outgrowth 2), also known as GPRIN2, is a 458 amino acid protein that is expressed in cerebellum and is thought to play a role in neurite outgrowth. GRIN2 interacts with activated G?oand G?, and is encoded by a gene that maps to human chromosome 10q11.22.

Supplier: Bioss

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.

Supplier: Bioss

G protein-coupled receptors (GPCRs) represent a large superfamily of cell-surface receptors that are involved in a multitude of physiological processes such as perception of sensory information, modulation of synaptic transmission, hormone release/actions, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesize intracellular second messengers, such as diacylglycerol, cyclic AMP, inositol phosphates and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling and are involved in many pathological conditions. GRIN2 (G protein-regulated inducer of neurite outgrowth 2), also known as GPRIN2, is a 458 amino acid protein that is expressed in cerebellum and is thought to play a role in neurite outgrowth. GRIN2 interacts with activated G?oand G?, and is encoded by a gene that maps to human chromosome 10q11.22.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.