Proteins & Peptides

BMP2K or Bone morphogenic protein 2 inducible kinase is the human homolog of mouse BMP-2-inducible kinase which plays a key role in skeletal development and patterning. BMP2K is a serine/threonine protein kinase which contains a nuclear localization signal and plays a regulatory role in attenuating the program of osteoblast differentiation. BMP2K gene is strongly correlated with high myopia and may contribute to a genetic risk factor for high degrees of myopic pathogenesis (1). BMP-2 expression is suppressed by an EP4 receptor antagonist and PGE2 produced by COX-2 increases BMP-2 expression via binding the EP4 receptor (2). BMP2K Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, JNK/SAPK Pathway, NfkB Pathway, p38 Pathway, PKA/PKC Pathway, and WNT Signaling research.

BUB1 is a kinase which involved in spindle checkpoint function that in part by phosphorylating a member of the miotic checkpoint complex and activating the spindle checkpoint. BUB1 is highly expressed in thymus, ovary, and testis (1). BUB1 maintains the steady-state level and centromeric localization of SGO1, and they concluded that BUB1 protects centromeric cohesion in mitosis through SGO1 (2). BUB1-mediated phosphorylation of CDC20 is required for proper checkpoint signaling and that inhibition of APC by BUB1 may partly account for the sensitivity of the spindle checkpoint. BUB1 kinase creates a mark for shugoshin localization and the correct partitioning of chromosomes. BUB1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

BUB1 is a kinase which involved in spindle checkpoint function that in part by phosphorylating a member of the miotic checkpoint complex and activating the spindle checkpoint. BUB1 is highly expressed in thymus, ovary, and testis (1). BUB1 maintains the steady-state level and centromeric localization of SGO1, and they concluded that BUB1 protects centromeric cohesion in mitosis through SGO1 (2). BUB1-mediated phosphorylation of CDC20 is required for proper checkpoint signaling and that inhibition of APC by BUB1 may partly account for the sensitivity of the spindle checkpoint. BUB1 kinase creates a mark for shugoshin localization and the correct partitioning of chromosomes. BUB1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, Cell Cycle, and Ser/Thr Kinases research.

Calmodulin 1 is a member of calcium-modulated proteins which is present in the cytosol and on membranes facing the cytosol and has a high affinity for calcium. Calmodulin 1 has 4 calcium-binding domains and plays a role in cell growth, cell cycle, signal transduction and the synthesis and release of neurotransmitters. Calmodulin can bind to the epidermal growth factor receptor at its cytosolic juxtamembrane region and this inhibits its tyrosine kinase activity (1). A number of other proteins including HSP70 have been shown to interact with Calmodulin 1 in a cell-phase-specific manner (2). Calmodulin 1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, and PKA/PKC Pathway research.

Calmodulin 1 is a member of calcium-modulated proteins which is present in the cytosol and on membranes facing the cytosol and has a high affinity for calcium. Calmodulin 1 has 4 calcium-binding domains and plays a role in cell growth, cell cycle, signal transduction and the synthesis and release of neurotransmitters. Calmodulin can bind to the epidermal growth factor receptor at its cytosolic juxtamembrane region and this inhibits its tyrosine kinase activity (1). A number of other proteins including HSP70 have been shown to interact with Calmodulin 1 in a cell-phase-specific manner (2). Calmodulin 1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, and PKA/PKC Pathway research.

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.

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.

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.