You Searched For: Ferroceneboronic+acid

Catalog Number: (76084-884)

Supplier: Bioss

Description: PPP1A is a serine/threonine protein phosphatase catalytic subunit that is essential for regulating cellular stress responses in eukaryotes. It binds to magnesium or manganese ions and exists as a monomer. It is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. PPP1A is involved in the regulation long term synaptic plasticity and may play an important role in dephosphorylating substrates such as Ca2+/calmodulin dependent protein kinase II.

Catalog Number: (10496-322)

Supplier: Bioss

Description: The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. TSSK 6 (testis-specific serine kinase 6), also known as SSTK, TSSK4, FKSG82 or CT72, is a 273 amino acid protein that contains one protein kinase domain and belongs to the Ser/Thr protein kinase family. Highly expressed in testis with lower expression in ovary, colon, thymus, small intestine and spleen, TSSK 6 catalyzes the ATP-dependent phosphorylation of proteins involved in sperm production and chromatin remodeling. TSSK 6 uses magnesium as a cofactor and is thought to be required for proper sperm development and function, as well as DNA condensation events. Defects in the gene encoding TSSK 6 are associated with male infertility characterized by low sperm count and decreased sperm motility.

Catalog Number: (10496-324)

Supplier: Bioss

Description: The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. TSSK 6 (testis-specific serine kinase 6), also known as SSTK, TSSK4, FKSG82 or CT72, is a 273 amino acid protein that contains one protein kinase domain and belongs to the Ser/Thr protein kinase family. Highly expressed in testis with lower expression in ovary, colon, thymus, small intestine and spleen, TSSK 6 catalyzes the ATP-dependent phosphorylation of proteins involved in sperm production and chromatin remodeling. TSSK 6 uses magnesium as a cofactor and is thought to be required for proper sperm development and function, as well as DNA condensation events. Defects in the gene encoding TSSK 6 are associated with male infertility characterized by low sperm count and decreased sperm motility.

Catalog Number: (10071-870)

Supplier: Prosci

Description: This is a calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. Essential for T-cell receptor (TCR)-mediated T-cell activation, but is dispensable during TCR-dependent thymocyte development. Links the TCR signaling complex to the activation of NF-κ-B in mature T lymphocytes. Required for interleukin-2 (IL2) production. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.

Catalog Number: (10366-260)

Supplier: Bioss

Description: This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].

Catalog Number: (10366-258)

Supplier: Bioss

Description: This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].

Catalog Number: (10401-392)

Supplier: Bioss

Description: This is a calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. Essential for T-cell receptor (TCR)-mediated T-cell activation, but is dispensable during TCR-dependent thymocyte development. Links the TCR signaling complex to the activation of NF-kappa-B in mature T lymphocytes. Required for interleukin-2 (IL2) production.PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.

Catalog Number: (10421-082)

Supplier: Bioss

Description: Rsk1 is a member of a family of 90kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases activated in response to mitogenic stimuli, including extracellular signal regulated protein kinases Erk1 and Erk2. Rsk1 is activated by MAPK in vitro and in vivo via phosphorylation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Catalog Number: (CAPIPA5-14955)

Supplier: Thermo Scientific

Description: RIPK3 is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.

Catalog Number: (CAPIPA5-13759)

Supplier: Thermo Scientific

Description: AKT2 is a putative oncogene encoding a protein belonging to a subfamily of serine/threonine kinases containing SH2-like (Src homology 2-like) domains. Furthermore, AKT2 was shown to be amplified and overexpressed in 2 of 8 ovarian carcinoma cell lines and 2 of 15 primary ovarian tumors. Overexpression of AKT2 contributes to the malignant phenotype of a subset of human ductal pancreatic cancers. AKT2 is a general protein kinase capable of phophorylating several known proteins.

Supplier: Enzo Life Sciences

Description: Calcineurin is a Ca2+/Calmodulin-dependent serine/threonine protein phosphatase. The active enzyme is a heterodimer consisting of a catalytic A subunit and a myristylated regulatory B subunit that binds calcium. Calcineurin, which is the target of immunosuppressant drugs such as cyclosporin A and FK506, controls the translocation of Nuclear factors of activated T-cells (NFAT), a family of transcriptional activators that control the expression of cytokine genes essential to immune response, from the cytosol into the nucleus of activated T-cells.

SDS

Catalog Number: (76082-820)

Supplier: Bioss

Description: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. Required for atypical chemokine receptor ACKR2-induced phosphorylation of cofilin (CFL1).

Catalog Number: (10366-252)

Supplier: Bioss

Description: This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].

Catalog Number: (10369-340)

Supplier: Bioss

Description: This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].

Catalog Number: (10338-784)

Supplier: Bioss

Description: p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

Catalog Number: (77438-992)

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.