125958 Results for: "3-Carbamoyl-5-fluorobenzeneboronic+acid"

Supplier: Bioss

Receptor for GABA. The activity of this receptor is mediated by G-proteins that inhibit adenylyl cyclase activity, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipids hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA-B-R inhibit neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA-B-R decrease neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA ) and metabotropic (GABAB ) receptors as well as a third class of receptors called GABAC. In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton. The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA ) and metabotropic (GABAB ) receptors as well as a third class of receptors called GABAC. In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton. The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA ) and metabotropic (GABAB ) receptors as well as a third class of receptors called GABAC. In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton. The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex.

Supplier: Bioss

The Vang family of proteins are integral membrane proteins that are homologues of the Drosophila tissue polarity gene strabismus. The gene encoding for Van Gogh-like protein 1 (Vangl1), also designated Strabismus 2 (STB2), localizes to human chromosome 1p11-p13.1. Van Gogh-like protein 2 (Vangl2), also designated Strabismus 1 (STB1), localizes to chromosome 1q22-q23. Vangl1 is expressed primarily in testis and ovary, but is also expressed in gastric and pancreatic cancer. Vangl proteins play a key developmental role in establishing planar cell polarity (PCP) and in regulating convergent extension (CE) movements during embryogenesis. Vangl1 and Vangl2 are both downregulated in several cancer cell lines and primary tumors.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: UVEX

This chemical protection glove features a double cotton-interlock lining. This means that the rubiflex SNB35SF is suitable for a wide range of applications that require chemical protection in addition to increased mechanical protection to heat and cold.

Supplier: MACHEREY-NAGEL

Photometric test kits for the determination of cyanide in water samples.

Supplier: Alla France

These certified thermometers are manufactured using a type N 16 soda lime glass with diameter ~6 to 7 mm.

Supplier: Bioss

Receptor for GABA. The activity of this receptor is mediated by G-proteins that inhibit adenylyl cyclase activity, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipids hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA-B-R inhibit neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA-B-R decrease neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

Supplier: Bioss

The Vang family of proteins are integral membrane proteins that are homologues of the Drosophila tissue polarity gene strabismus. The gene encoding for Van Gogh-like protein 1 (Vangl1), also designated Strabismus 2 (STB2), localizes to human chromosome 1p11-p13.1. Van Gogh-like protein 2 (Vangl2), also designated Strabismus 1 (STB1), localizes to chromosome 1q22-q23. Vangl1 is expressed primarily in testis and ovary, but is also expressed in gastric and pancreatic cancer. Vangl proteins play a key developmental role in establishing planar cell polarity (PCP) and in regulating convergent extension (CE) movements during embryogenesis. Vangl1 and Vangl2 are both downregulated in several cancer cell lines and primary tumors.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing (1). GABA has been shown to activate both ionotropic (GABAA) and metabotropic (GABAB) receptors as well as a third class of receptors called GABAC (2,3). In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein) (4-6). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton (6). The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex (6).

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

Receptor for GABA. The activity of this receptor is mediated by G-proteins that inhibit adenylyl cyclase activity, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipids hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA-B-R inhibit neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA-B-R decrease neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

Supplier: Bioss

CBG is a monomeric enzyme involved in the absorption and metabolism of flavonoid glucosides. CBG is found predominately in the liver, but is also located in tissues such as spleen, small intestine and kidney. Through its catalytic activity, CBG is able to hydrolyze a variety of glycosides including phytoestrogens, cyanogens, and flavonols. Although its catalytic activity extends to many dietary flavonoids, CBG has increased specificity for hydrophobic aglycones such as beta-D-glucoside and beta-D-galactoside. Hydrolysis is inhibited by sodium taurocholate and glucosyl-sphingosine, both of which regulate CBG enzymatic activity. Deficiencies in CBG have been implicated in Gaucher’s disease, a lysosomal storage disease that causes a build up of fatty material in the spleen, liver, lung and kidneys.

Supplier: Bioss

The Vang family of proteins are integral membrane proteins that are homologues of the Drosophila tissue polarity gene strabismus. The gene encoding for Van Gogh-like protein 1 (Vangl1), also designated Strabismus 2 (STB2), localizes to human chromosome 1p11-p13.1. Van Gogh-like protein 2 (Vangl2), also designated Strabismus 1 (STB1), localizes to chromosome 1q22-q23. Vangl1 is expressed primarily in testis and ovary, but is also expressed in gastric and pancreatic cancer. Vangl proteins play a key developmental role in establishing planar cell polarity (PCP) and in regulating convergent extension (CE) movements during embryogenesis. Vangl1 and Vangl2 are both downregulated in several cancer cell lines and primary tumors.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA ) and metabotropic (GABAB ) receptors as well as a third class of receptors called GABAC. In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton. The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex.

Supplier: 3M

AdFlo™ Powered air respirator filter and battery kit contains the Adflo™ filter and Adflo™ heavy-duty Li-ion battery. It’s designed for use with 3M™ Adflo™ powered air respirator.

Supplier: Bioss

Receptor for GABA. The activity of this receptor is mediated by G-proteins that inhibit adenylyl cyclase activity, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipids hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA-B-R inhibit neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA-B-R decrease neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

The Vang family of proteins are integral membrane proteins that are homologues of the Drosophila tissue polarity gene strabismus. The gene encoding for Van Gogh-like protein 1 (Vangl1), also designated Strabismus 2 (STB2), localizes to human chromosome 1p11-p13.1. Van Gogh-like protein 2 (Vangl2), also designated Strabismus 1 (STB1), localizes to chromosome 1q22-q23. Vangl1 is expressed primarily in testis and ovary, but is also expressed in gastric and pancreatic cancer. Vangl proteins play a key developmental role in establishing planar cell polarity (PCP) and in regulating convergent extension (CE) movements during embryogenesis. Vangl1 and Vangl2 are both downregulated in several cancer cell lines and primary tumors.

Supplier: Bioss

Receptor for GABA. The activity of this receptor is mediated by G-proteins that inhibit adenylyl cyclase activity, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipids hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA-B-R inhibit neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA-B-R decrease neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Brand

Fixed volume or variable volume, analogue-adjustable or Digital Easy Calibration.

Supplier: Bioss

In the central nervous system GABA functions as the main inhibitory transmitter by increasing a Cl-conductance that inhibits neuronal firing. GABA has been shown to activate both ionotropic (GABAA ) and metabotropic (GABAB ) receptors as well as a third class of receptors called GABAC. In addition to GABA receptors, several proteins have been identified as regulators of GABA function, including GAD65, GAD67, GABA transporters and GABARAP (GABAA receptor-associated protein). GABARAP associates with GABAA Rg2 to link GABAA receptors to the cytoskeleton. The GABARAP protein sequence is similar to light chain-3 of microtubule-associated proteins (MAPs) suggesting that it may be a type of MAP or a component of a MAP complex.