195614 Results for: "Geological Processes Earth Science Lab Activities&amp"

Supplier: Bioss

The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Cyclin dependent kinase 5 (Cdk5) is a key regulator of cell cycle progression in neuronal differentiation that physically associates with and is activated by the neuron-specific protein p35. CDK5RAP1 (Cdk5 regulatory subunit-associated protein 1), also known as Cdk5 activator-binding protein C42, is a 601 amino acid protein that specifically inhibits Cdk5 activation by p35 through formation of a dimer that inhibits kinase activity. CDK5RAP1 contains one TRAM domain, which is thought to bind tRNA and deliver the RNA-modifying enzymatic domain to its target. There are 4 named isoforms of CDK5RAP1 that are produced as a result of alternative splicing events and are expressed at high levels in heart and skeletal muscle.

Supplier: Bioss

Cyclin dependent kinase 5 (Cdk5) is a key regulator of cell cycle progression in neuronal differentiation that physically associates with and is activated by the neuron-specific protein p35. CDK5RAP1 (Cdk5 regulatory subunit-associated protein 1), also known as Cdk5 activator-binding protein C42, is a 601 amino acid protein that specifically inhibits Cdk5 activation by p35 through formation of a dimer that inhibits kinase activity. CDK5RAP1 contains one TRAM domain, which is thought to bind tRNA and deliver the RNA-modifying enzymatic domain to its target. There are 4 named isoforms of CDK5RAP1 that are produced as a result of alternative splicing events and are expressed at high levels in heart and skeletal muscle.

Supplier: Prosci

Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.

Supplier: Bioss

E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription (By similarity).

Supplier: Prosci

Anexin A5 is a phospholipid binding protein, which binds with high affinity and selectivity to PS in the presence of calcium. PS is predominantly located in membrane leaflets, which face the cytosol. However, recent findings show that each cell type has the molecular machinery to expose PS at its cell surface. This machinery is activated during the execution of apoptosis. Once PS is exposed at the cell surface it exhibits procoagulant and proinflammatory activities. Anexin A5 will bind to the PS-exposing apoptotic cell and can inhibit the procoagulant and proinflammatory activities of the dying cell. Anexin A5 has also been identified as an anticoagulant protein in the blood coagulation cascade, by acting as an inhibitor of prothrombin activation. The presence of antibodies to Anexin A5 is associated with systemic lupus erythematosus (SLE), recurrent spontaneous abortions and systemic sclerosis (SSc).

Supplier: Bioss

E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription (By similarity).

Supplier: Prosci

Mouse Ifng is a secreted protein which belongs to the type I I (or gamma) interferon family. IFNG is produced by lymphocytes and activated by specific antigens or mitogens. In addition to having antiviral activity, IFNG also has important immunoregulatory functions. It is a potent activator of macrophages and has antiproliferative effects on transformed cells. It can potentiate the antiviral and antitumor effects of the type I interferons. Genetic variation in IFNG is associated with the risk of aplastic anemia (AA) which is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis.

Supplier: Prosci

KLRA1 Antibody: KLRA1 (also known and Ly49L) is a member of the LY49 family of receptors Natural killer (NK) cells that bind to major histocompatibility complex (MHC) class 1. These proteins are classified as either activating or inhibitory receptors based on whether they possess an immunoreceptor tyrosine-based inhibitory motif (ITIM) in their cytoplasmic region (for inhibitory receptors), or an immunoreceptor tyrosine-based activation motif (ITAM) that transmits activating signals resulting in phosphorylation of several substrates. KLRA1 is thought to be an activating receptor, inducing DAP12 phosphorylation in response to antibody-mediated cross-linking of KLRA1 on NK cells. At least three isoforms of KLRA1 are known to exist.

Supplier: ARLINK DIVISION CUST SERV TE

The starter assembly is the first component for each workstation and includes two columns with outer and inner trim, and a closed stabilizer panel. Optional open stabilizer panel may be ordered for full access from the rear of the workstation.

Supplier: Bioss

Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.

Supplier: Bioss

Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.

Supplier: Bioss

Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.

Supplier: Bioss

Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.

Supplier: Bioss

This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Supplier: Bioss

Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.

Supplier: Bioss

Receptor for oxytocin. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system.

Supplier: Bioss

This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Supplier: Bioss

This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Supplier: Bioss

The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

Supplier: Bioss

The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

Supplier: Bioss

Bid, a BH3 domain containing proapoptotic Bcl2 family member, is localized in the cytosolic fraction of cells as an inactive precursor. Its active form is generated upon proteolytic cleavage by caspase 8 in the Fas signaling pathway. Cleaved Bid translocates to mitochondria and releases its potent proapoptotic activity, which in turn induces cytochrome c release and mitochondrial damage. The cytochrome c releasing activity of Bid was antagonized by Bcl2. Mutation in the SH3 domain can diminish the cytochrome c releasing activity. In animal model studies, Bid deficient mice are found resistant to the lethal effects of death factor signals relayed through Fas.

Supplier: Bioss

RSK3(Ribosomal S6 kinase 3)is a member of a family of 90-kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases that are activated in response to mitogenic stimuli, including extracellular signal-regulated protein kinases Erk1 and Erk2. Rsk3 is a distinct isoform of p90Rsk that translocates to the cell nucleus, phosphorylates potential nuclear targets and may have a unique upstream activator. Several sites, such as Ser380, Thr359, Ser363 and Thr573, are important for its activation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Supplier: Prosci

Pellino 1 Antibody: The Pellino proteins are a highly homologous family of E3 ubiquitin ligases that act as upstream mediators in Toll-like receptor (TLR) pathways that lead to activation of MAP kinases and transcription factors. Pellino 1 is required for interleukin-1-mediated signaling through its interaction with the IRAK4-IRAK-TRAF6 complex, ultimately resulting in the activation of NF-kappa B. Like other members of the Pellino family, Pellino 1 is an E3 ubiquitin ligase, able to catalyze the polyubiquitination of IRAK1. It is activated via phosphorylation by either IRAK1 and IRAK4 or the IKK-related kinases IKK- epsilon and TBK1. In addition to phosphorylation, Pellino 1 activity is also modulated via ubiquitination and sumoylation.

Supplier: Rockland Immunochemical

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.

Supplier: Rockland Immunochemical

The Pellino proteins are a highly homologous family of E3 ubiquitin ligases that act as upstream mediators in Toll-like receptor (TLR) pathways that lead to activation of MAP kinases and transcription factors. Pellino 1 is required for interleukin-1-mediated signaling through its interaction with the IRAK4-IRAK-TRAF6 complex, ultimately resulting in the activation of NF-kB. Like other members of the Pellino family, Pellino 1 is an E3 ubiquitin ligase, able to catalyze the polyubiquitination of IRAK1. It is activated via phosphorylation by either IRAK1 and IRAK4 or the IKK-related kinases IKK-e and TBK1. In addition to phosphorylation, Pellino 1 activity is also modulated via ubiquitination and sumoylation.

Supplier: Bioss

RSK3(Ribosomal S6 kinase 3)is a member of a family of 90-kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases that are activated in response to mitogenic stimuli, including extracellular signal-regulated protein kinases Erk1 and Erk2. Rsk3 is a distinct isoform of p90Rsk that translocates to the cell nucleus, phosphorylates potential nuclear targets and may have a unique upstream activator. Several sites, such as Ser380, Thr359, Ser363 and Thr573, are important for its activation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.

Supplier: Rockland Immunochemical

Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage by caspases 8, 9 and 10 to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins such as caspases 6, 7 and 9.

Supplier: Bioss

Protein S (PROS) is a vitamin K-dependent plasma protein that inhibits blood clotting by serving as a cofactor for activated protein C (APC) and facilitates clearance of early apoptotic cells. In the plasma, circulating Protein S becomes inactive upon complexing with C4b-binding protein (C4BP); 60 to 70% of Protein S circulates in complex with C4BP. Calcium-dependent association of C4BP-Protein S with apoptotic cells influences the regulation of complement activation. Protein S has APC-independent anticoagulant activity through direct inhibition of prothrombin activation via interactions with Factor X A, Factor V A and phospholipids. Autosomal dominant Protein S deficiency (levels 15 to 37% of normal) correlates with severe recurrent venous thrombosis.

Supplier: Bioss

RSK3(Ribosomal S6 kinase 3)is a member of a family of 90-kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases that are activated in response to mitogenic stimuli, including extracellular signal-regulated protein kinases Erk1 and Erk2. Rsk3 is a distinct isoform of p90Rsk that translocates to the cell nucleus, phosphorylates potential nuclear targets and may have a unique upstream activator. Several sites, such as Ser380, Thr359, Ser363 and Thr573, are important for its activation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.