You Searched For: N-Carbobenzoxy-L-threonine

Catalog Number: (10231-710)

Supplier: Bioss

Description: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.

Catalog Number: (10493-220)

Supplier: Bioss

Description: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression.

Catalog Number: (10493-218)

Supplier: Bioss

Description: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression.

Catalog Number: (10091-018)

Supplier: Proteintech

Description: NEK11(Serine/threonine-protein kinase) belongs to the NIMA family of kinases, which are involved in DNA replication and genotoxic stress responses.It controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation.It has 4 isoforms produced by alternative splicing.

Catalog Number: (76100-630)

Supplier: Bioss

Description: The p21 activated kinases (PAK) are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and RAC1, and have been implicated in a wide range of biological activities. The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in regulating the apoptotic events in the dying cell.P21-activated kinase (PAK) is actually a family of serine/threonine protein kinases, members of which are activated by small molecular weight GTPases. The three most common isoforms are PAK 1, PAK 2, and PAK 3 (also known as alpha PAK, gamma PAK, and beta PAK, respectively). These kinases contain numerous regulatory elements that trigger diverse signaling processes such as those initiated by activated GTPases, interaction with Src homology 3 (SH3) domains, and caspase mediated proteolytic cleavage. Autophosphorylation of serine 141 (serine 144 for PAK 1 and serine 139 PAK 3), catalyzed by Cdc42, is required for activation of PAK.

Catalog Number: (10411-202)

Supplier: Bioss

Description: The Raf kinases are important intermediates in signal transduction. Raf protein family members, including A Raf and B Raf, have intrinsic serine/threonine kinase activity. Interaction between Ras proteins and Raf proteins results in Raf-mediated phosphorylation and activation of MEK (also known as MAP kinase kinase). Defects in BRAF are involved in a wide range of cancers. B-Raf is a serine/threonine protein kinase that acts as a signal transducer from membrane-associated receptors to nuclear transcription factors. 1 BRAF is important for the regulation of cell proliferation and determination of cell fate during embryogenesis. BRAF acts downstream of Ras and upstream of MEK in the Ras-Raf-MEK-ERK signal transduction pathway, which is a conserved RAS-activated protein kinase cascade that regulates cell growth, proliferation, and differentiation in response to growth factors, cytokines, and hormones.

Catalog Number: (89415-358)

Supplier: Prosci

Description: RICK Antibody: Apoptosis is mediated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. DD-containing serine/threonine kinase RIP regulates Fas-induced apoptosis. A novel CARD-containing serine/threonine kinase was recently identified and designated RICK/RIP2/CARDIAK for RIP-like interacting CLARP kinase, receptor interacting protein-2, and CARD-containing ICE associated kinase, respectively. RICK contains an N-terminal kinase catalytic domain and a C-terminal CARD domain. Overexpression of RICK induced apoptosis and activation of NF-kappa B and JNK. RICK interacts with members of the TRAF family, CLARP and caspase-1. Thus, RICK represents a novel kinase that regulates TNF and Fas induced-apoptosis and that is involved in the generation of proinflammatory cytokine IL-1 beta. The messenger RNA of RICK is expressed in multiple human tissues.

Catalog Number: (89415-300)

Supplier: Prosci

Description: RICK Antibody: Apoptosis is mediated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. DD-containing serine/threonine kinase RIP regulates Fas-induced apoptosis. A novel CARD-containing serine/threonine kinase was recently identified and designated RICK/RIP2/CARDIAK for RIP-like interacting CLARP kinase, receptor interacting protein-2, and CARD-containing ICE associated kinase, respectively. RICK contains an N-terminal kinase catalytic domain and a C-terminal CARD domain. Overexpression of RICK induced apoptosis and activation of NF-kappa B and JNK. RICK interacts with members of the TRAF family, CLARP and caspase-1. Thus, RICK represents a novel kinase that regulates TNF and Fas induced-apoptosis and that is involved in the generation of proinflammatory cytokine IL-1 beta. The messenger RNA of RICK is expressed in multiple human tissues.

Catalog Number: (10411-206)

Supplier: Bioss

Description: The Raf kinases are important intermediates in signal transduction. Raf protein family members, including A Raf and B Raf, have intrinsic serine/threonine kinase activity. Interaction between Ras proteins and Raf proteins results in Raf-mediated phosphorylation and activation of MEK (also known as MAP kinase kinase). Defects in BRAF are involved in a wide range of cancers. B-Raf is a serine/threonine protein kinase that acts as a signal transducer from membrane-associated receptors to nuclear transcription factors. 1 BRAF is important for the regulation of cell proliferation and determination of cell fate during embryogenesis. BRAF acts downstream of Ras and upstream of MEK in the Ras-Raf-MEK-ERK signal transduction pathway, which is a conserved RAS-activated protein kinase cascade that regulates cell growth, proliferation, and differentiation in response to growth factors, cytokines, and hormones.

Catalog Number: (10411-204)

Supplier: Bioss

Description: The Raf kinases are important intermediates in signal transduction. Raf protein family members, including A Raf and B Raf, have intrinsic serine/threonine kinase activity. Interaction between Ras proteins and Raf proteins results in Raf-mediated phosphorylation and activation of MEK (also known as MAP kinase kinase). Defects in BRAF are involved in a wide range of cancers. B-Raf is a serine/threonine protein kinase that acts as a signal transducer from membrane-associated receptors to nuclear transcription factors. 1 BRAF is important for the regulation of cell proliferation and determination of cell fate during embryogenesis. BRAF acts downstream of Ras and upstream of MEK in the Ras-Raf-MEK-ERK signal transduction pathway, which is a conserved RAS-activated protein kinase cascade that regulates cell growth, proliferation, and differentiation in response to growth factors, cytokines, and hormones.

Catalog Number: (10391-392)

Supplier: Bioss

Description: Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Catalog Number: (10391-378)

Supplier: Bioss

Description: Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Catalog Number: (10391-400)

Supplier: Bioss

Description: Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Catalog Number: (10231-724)

Supplier: Bioss

Description: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.

Catalog Number: (10467-696)

Supplier: Bioss

Description: This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, thymus, fetal liver, and carcinomas. Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN.

Catalog Number: (10472-908)

Supplier: Bioss

Description: Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly.Tissue specificity: Widely expressed. Present in fetal placenta, liver, kidney, pancreas, heart and skeletal muscle. Also found in adult cell lines.