"SR-12813&amp"

Supplier: Honeywell Chemicals

Certified Reference Material (CRM).

Supplier: Honeywell Chemicals

Coulometric Karl Fischer titrations normally require two reagent solutions: an anolyte (the solution in the anodic compartment) and a catholyte (the solution in the cathodic compartment).

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: US Biological

Anti-PNN Rabbit Polyclonal Antibody

Supplier: Bioss

Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKMY1 (ankyrin repeat and MYND domain containing 1), also known as ZMYND13 or TSAL1, is a 941 amino acid protein that contains seven ANK repeats, three MORN repeats and one MYND-type zinc finger. MORN repeats were first identified in junctophilins, cytoplasmic proteins involved in junctions between the plasma membrane and the ER/SR membrane. The presence of MORN repeats suggests that ANKMY1 may interact with the plasma membrane. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif which may be involved in protein-protein interactions. Three isoforms of ANKMY1 exists due to alternative splicing events.

Supplier: Biorbyt

Anti-PRKAA2 Rabbit Polyclonal Antibody

Supplier: US Biological

Anti-SRSF10 Mouse Monoclonal Antibody [clone: 1A6]

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: ProSci Inc.

TNPO3 Antibody: TNPO3 is a member of the importin beta/transportin family of nuclear import receptors and is specific for the essential splicing factors termed SR proteins, binding specifically and directly to the arginine/serine (RS)-rich domains of these proteins. Further experiments demonstrated that this interaction occurs only when these RS domains are phosphorylated. More recently, TNPO3 was identified as an HIV dependency factor (HDF) and that depletion of TNPO3 resulted in HIV inhibition after reverse transcription but before integration, suggesting that TNPO3 may be an important drug target in HIV treatment. At least three isoforms of TNPO3 are known to exist.

Supplier: ProSci Inc.

TNPO3 Antibody: TNPO3 is a member of the importin beta/transportin family of nuclear import receptors and is specific for the essential splicing factors termed SR proteins, binding specifically and directly to the arginine/serine (RS)-rich domains of these proteins. Further experiments demonstrated that this interaction occurs only when these RS domains are phosphorylated. More recently, TNPO3 was identified as an HIV dependency factor (HDF) and that depletion of TNPO3 resulted in HIV inhibition after reverse transcription but before integration, suggesting that TNPO3 may be an important drug target in HIV treatment. At least three isoforms of TNPO3 are known to exist.

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: ProSci Inc.

CCDC55 Antibody: CCDC55, also known as Nuclear speckle-related protein 70 (NSrp70), was initially identified by the NIH Mammalian Gene Collection. Nuclear speckles are known to be the storage sites of mRNA splicing regulators. CCDC55 has been suggested to modulate alternative pre-mRNA splicing in vivo. It co-localizes and physically interacts with the SR proteins SC35 and ASF/SF2, essential splicing factors which are required for constitutive splicing and can regulate alternative mRNA splicing. Loss of CCDC55 in mice leads to early embryonic lethality highlights the importance of the functional role of CCDC55.

Supplier: Biorbyt

Anti-PPP1R1B Rabbit Polyclonal Antibody