Other Proteins

CaMKPase is a member of the PP2C family of Ser/Thr protein phosphatases that dephosphorylate and regulate the multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs) (1). The multifunctional CaMKs mediate cellular responses induced by increases in second messenger Ca2+ and have been implicated in the control of synaptic transmission, gene transcription, cell growth and contraction of cardiac and smooth muscles (2). Overexpression of CaMKPase has been shown to mediate caspase-dependent apoptosis. CaMKPase can also interact with the Rho guanine nucleotide exchange factors (PIX) thereby blocking the effects of p21-activated kinase 1 (PAK1). CaMKPase Protein is ideal to investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, Phosphatases, and PKA/PKC Pathway research.

Catenin α is a novel actin-binding and -bundling protein. Catenin α is responsible for organizing and tethering actin filaments at the zones of E-cadherin-mediated cell-cell contact (1). Monomeric Catenin α can bind strongly to E-Cadherin-β-Catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that Catenin α is an allosteric protein. Catenin α directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments (2). Catenin α Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Cancer, Cardiovascular Disease, Invasion/Metastasis, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

β-catenins are cytoplasmic proteins that are ubiquitously expressed. These proteins associate with E-cadherin at cellular junctions (1). β-catenin interacts with TCF and LEF transcription factors and is an essential member of the Wingless-Wnt signal transduction pathway. The adenomatous polyposis coli (APC) tumor-suppressor protein, together with Axin and GSK3β, form a Wnt-regulated signaling complex that mediates phosphorylation-dependent degradation of β-catenin by the proteasome. APC and Siah-1 mediate a novel β-catenin degradation pathway linking p53 activation to cell cycle control. Activating mutations in the human β-catenin gene have been found in human colon cancer and melanomas (2). Catenin β Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Cancer, Cardiovascular Disease, Invasion/Metastasis, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

CBP or CREB-binding protein is a nuclear transcriptional coactivator protein that binds specifically to the PKA-phosphorylated form of the CREB protein. Microinjection of an anti-CBP antiserum into fibroblasts leads to inhibition of transcription from a cAMP promoter (1). CBP can also cooperates with upstream activators, such as JUN. When JUN is phosphorylated at the transcriptionally stimulatory sites ser73 and ser63, it binds CBP with comparable affinity to CREB. Insulin signaling may directly regulate many cAMP signaling pathways at the transcriptional level by controlling CBP recruitment (2). Mutant CBP can be aberrantly recruited to CREB protein, resulting in inappropriate activation of gluconeogenesis and glucose intolerance. CBP Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Apoptosis/Autophagy, Cardiovascular Disease, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway,and PKA/PKC Pathwa

CDC7 is a cell division cycle protein that is critical for the G1/S transition and initiation of DNA replication during the cell division cycle. Overexpression of CDC7 gene product may be associated with neoplastic transformation for some tumors. Inhibition of CDC7 in cancer cells impairs progression through S phase, inducing a p53-independent apoptotic cell death, whereas in normal cells, it does not affect cell viability (1). Inhibition of CDC7 kinase activity in cancer cells restricts DNA replication and induces apoptosis. CDC7 phosphorylates the minichromosome maintenance protein 2 (Mcm2), a component of the DNA replicative helicase needed for genome duplication (2). CDC7 Protein is ideal for investigators involved in Signaling Proteins, Cell-Cycle Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

CDC2L1 is a member of the p34Cdc2 protein kinase family. p34Cdc2 protein kinase family is known to be essential for eukaryotic cell cycle control. CDC2L1 is well conserved evolutionarily and is regulated during murine embryogenesis. CDC2L1 activity is coordinately regulated with that of p34 (cdc2) during the cell cycle (1). The protein kinase encoded by CDC2L1 can be cleaved by caspases and is demonstrated to play roles in cell apoptosis (2). CDC2L1 Protein is ideal for investigators involved in Signaling Proteins, Cell Cylce Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

CDK2 is a member of the Cyclin-Dependent Kinase family that is ubiquitously expressed. CDK2 is a catalytic subunit of the cyclin-dependent protein kinase complex, whose activity is restricted to the G1-S phase, and essential for cell cycle G1/S phase transition. CDK2 associates with and is regulated by the regulatory subunits of the complex including Cyclin A or E, CDK inhibitor p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B) (1). CDK2 phosphorylates multiple cellular substrates including SMAD3 and FOXO1. Phosphorylation of FOXO1 leads to its inhibition (2). CDK2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

CDK5P25 (cyclin-dependent kinase 5, regulatory subunit 1) is a neuron-specific activator of CDK5 and is required for proper development of the central nervous system (1). The p35 form of this protein is proteolytically cleaved by calpain, generating a p25 form of the protein which relocates from the cell periphery to nuclear and perinuclear regions. CDK5P25 regulates CDK5 activity by prolonging its activation and changing its cellular location and this may be important in pain signaling (2). The CDK5P25 accumulates in the brain neurons of patients with Alzheimer's disease and this accumulation correlates with an increase in CDK5 kinase activity which may result in aberrantly phosphorylated forms of the microtubule-associated protein tau. CDK5P25 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

CDK5P35 is a neuron-specific activator of cyclin-dependent kinase 5 (CDK5) that bind to cyclin to form active holoenzymes that play a pivotal role in the regulation of the eukaryotic cell cycle .The activation of CDK5 is required for proper development of the central nervous system. p35 is a regulatory subunit for CDK5 which is proteolytically cleaved by calpain and generating a p25 form that involved in the pathogenesis of cytoskeletal abnormalities and neuronal death in neurodegenerative diseases (1). Cdk/p35 plays a role in primary afferent nociceptive signaling and is required for cortical plate neurons to migrate past preexisting neurons and take up superficial positions to constitute the inside-outside layering order of cortical lamination(2). CDK5P35 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.