Proteins & Peptides

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.

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 Pathw

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

CDC42 is a member of the Rho family of GTPases and is part of cellular pathways fundamental to growth, differentiation and apoptosis (1). Downstream targets for CDC42 include those that regulate the actin cytoskeleton (e.g. WASP) and cellular stress pathways (e.g. PAK) as well as the coatomer protein complex and PAR6. CDC42 is involved in the G(1)-S progression of the cell cycle. CDC42 and its downstream effector mDia3 are involved in bi-orientation and stabilization of spindle microtubules attachment to kinetochores and regulate chromosome alignment and segregation during mitosis (2). CDC42 Protein is ideal for investigators involved in Signaling Proteins, G-Proteins, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, and Neurobiology research.

CDC42 is a member of the Rho family of GTPases and is part of cellular pathways fundamental to growth, differentiation and apoptosis (1). Downstream targets for CDC42 include those that regulate the actin cytoskeleton (e.g. WASP) and cellular stress pathways (e.g. PAK) as well as the coatomer protein complex and PAR6. CDC42 is involved in the G(1)-S progression of the cell cycle. CDC42 and its downstream effector mDia3 are involved in bi-orientation and stabilization of spindle microtubules attachment to kinetochores and regulate chromosome alignment and segregation during mitosis (2). CDC42 Protein is ideal for investigators involved in Signaling Proteins, G-Proteins, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, and Neurobiology research.

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.

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.