"mthlcyclohexanol&amp"

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.

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.

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.

Supplier: Biosensis

Adenylate cyclases are enzymes which interact with and are activated by the GTP bound alpha subunits of trimeric G-proteins. Activated adenylate cyclases are responsible for the production of the important "second messenger" signalling molecule cyclic-AMP, which is generated from ATP. The type III adenylate cyclase enzyme is localized in the membranes surrounding the cilia in neurons, and our antibody is an excellent marker of neuronal cilia in the brain and in cells in tissue culture. Adenylate cyclase type III is a large complex molecule of, in the human, 1145 amino acids with a deduced molecular weight of 129kDa. The protein may be variably glycosylated, so that on SDS-PAGE and western blots it runs as a diffuse band of about 160kDa in cortex and about 200kDa in olfactory epithelium. The molecule has a complex structure, with 12 transmembrane domains and two cyclase domains. Each cyclase domain is immediately C-terminal to 6 transmembrane segments, but only the second, C-terminal cyclase is believed to be catalytically active.

Supplier: Biorbyt

Anti-PRKAA2 Rabbit Polyclonal Antibody

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Cyclic AMP-regulated gene expression frequently involves a DNA element designated the cAMP-regulated enhancer (CRE). Many transcription factors bind to this element, including the protein CREB which is activated as a result of phosphorylation by protein kinase A. It has been shown that protein kinase A-mediated CREB phosphorylation results in its binding to a nuclear protein designated CBP (for CREB-binding protein). These findings suggest that CBP has many of the properties expected of a CREB co-activator. Another high molecular weight transcriptional adapter protein, designated p300, is characterized by three cysteine- and histidine-rich regions, of which the most carboxy terminal region specifically binds the adenovirus E1A protein. p300 molecules lacking an intact E1A binding site bypass E1A repression even in the presence of high concentrations of E1A. Sequence analysis of CBP and p300 has revealed substantial homology, arguing that these proteins are members of a conserved family of co-activators.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Biorbyt

Anti-PPP1R1B Rabbit Polyclonal Antibody

Supplier: AbFrontier

Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

Supplier: Biorbyt

Anti-PRKAG2 Rabbit Polyclonal Antibody

Supplier: AbFrontier

Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

Supplier: ProSci Inc.

PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.

Supplier: ProSci Inc.

PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.

Supplier: Biorbyt

Anti-PRKAG2 Rabbit Polyclonal Antibody