19545 Results for: "Sodium+carbonate+decahydrate"

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Rift Valley Fever Virus Nucleocapsid Antibody: Rift Valley Fever (RFV) virus is an arthropod-borne virus endemic to Africa that infects humans and animals that is transmitted predominantly by mosquitoes. During human infections, symptoms can range from benign fever to severe encephalitis and fatal hepatitis with hemorrhagic fever. The Bunyaviridae family of viruses to which the RVF virus belongs are spherical enveloped viruses with a tripartite RNA genome of negative or ambisense polarity. The three segments are referred to as the L, M, and S segments. The L and M segments are negative polarity and code fore the L-dependent RNA polymerase and glycoprotein precursor respectively. The S segment is of ambisense polarity and encodes the nucleoprotein and non-structural proteins.

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These tips are made of high quality, 100% pure, virgin medical grade PP. Made in the highest quality moulds, these tips can be used whenever the work demands a higher standard.

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SncA is a member of the synuclein family of structurally related proteins that are prominently expressed in the central nervous system, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and SncA and Snc-Beta inhibit phospholipase D2 selectively. SncA may serve to integrate presynaptic signaling and membrane trafficking. Aggregated SncA proteins form brain lesions that are hallmarks of neurodegenerative synucleinopathies. Defects in SncA play a role in the pathogenesis of Parkinson disease. SncA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer disease. SncA shares 95% sequence homology with rat SncA. Rat SncA is specifically expressed in brain and is associated with synaptosomal membranes in neurons

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ATM encoded by this gene belongs to the PI3/PI4-kinase family. This protein is an important cell cycle checkpoint kinase that phosphorylates; thus, it functions as a regulator of a wide variety of downstream proteins, including tumor suppressor proteins p53 and BRCA1, checkpoint kinase CHK2, checkpoint proteins RAD17 and RAD9, and DNA repair protein NBS1. This protein and the closely related kinase ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability. Mutations in this gene are associated with ataxia telangiectasia, an autosomal recessive disorder. Two transcript variants encoding different isoforms have been found for this gene.

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Serine/threonine kinase required for the mitogen or stress-induced phosphorylation of the transcription factors CREB (cAMP response element-binding protein) and ATF1 (activating transcription factor-1). Essential role in the control of RELA transcriptional activity in response to TNF. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and epidemal growth-factor (EGF), which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 14 (HMG-14).

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RET (ret proto-oncogene) is a member of the cadherin superfamily and a receptor tyrosine kinase, which are cell-surface molecules that transduce signals for cell growth and differentiation. It can undergo oncogenic activation in vivo and in vitro by cytogenetic rearrangement. Ligands that bind the Ret receptor include the glial cell line-derived neurotropic factor (GDNF) and its congeners neurturin, persephin and artemin. Alterations in the corresponding Ret gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma and a congenital developmental disorder known as Hirschsprung’s disease. The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr905 dramatically inhibits Ret autophosphorylation activity.

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GRASP (GRP1-associated scaffold protein, tamalin) is a 395 amino acid proteinencoded by the human gene GRASP. GRASP is a scaffold protein that com-prises multiple protein-interacting domains, including a 95 kDa postsynapticdensity protein (PSD-95)/discs-large/ZO-1 (PDZ) domain, a leucine-zipperregion and a carboxyl-terminal PDZ-binding motif. GRASP is involved withintracellular trafficking and contributes to the macromolecular organizationof group 1 metabotropic glutamate receptors (mGluRs) at synapses. GRASPforms a heteromer composed of GRASP , PSCD2 and at least one mGluR-1. Italso interacts with PSCD3, mGluR-2, mGluR-3 and mGluR-5. GRASP is highlyexpressed in brain and has lower levels of expression in lung, heart, embryo, kidney and ovary.

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This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats and is localized in the nucleus.

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The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation

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NFKB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NFKB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-κ-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-κ-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth.

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Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by HDAC5 belongs to the class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.

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IL-15RA Antibody: Interleukin 15 (IL-15RA) is a cytokine receptor that specifically binds IL-15 with high affinity. IL-15 regulates T and natural killer cell activation and proliferation. The IL-15 and IL-2 receptors share two subunits, IL-2R beta and IL-2R gamma, and IL-15RA is structurally related to IL-2RA, an additional IL-2-specific alpha subunit necessary for high affinity IL-2 binding. Unlike IL-2RA, IL-15RA is capable of binding IL-15 with high affinity independent of the other subunits. IL-15RA is thought to enhance cell proliferation and expression of apoptosis inhibitor Bcl-xL and Bcl-2.

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Adducins are a family of cytoskeleton proteins encoded by three genes (alpha, beta, gamma). Adducin is a heterodimeric protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Alpha- and gamma-adducins are ubiquitously expressed. In contrast, beta-adducin is expressed at high levels in brain and hematopoietic tissues. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing results in multiple variants encoding distinct isoforms; however, not all variants have been fully described.

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F-box only protein 9 (also called FBOX9 and Fbp9) is a member of the F-box protein family, which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternative splicing of this gene generates at least 3 transcript variants diverging at the 5' terminus. Isoform 1 is distinct from isoforms.

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Toll-like receptors (TLRs) play an essential role in the detection and elimination of invading microbes. They are type-1 transmembrane receptors, containing extracellular leucine rich repeats and an intracellular Toll/interleukin-1 receptor (TIR) domain. Upon stimulation, these receptors interact with specific TIR domain-containing adaptor proteins. Five such adaptors have been discovered to date, MyD88, Mal (MyD88 adaptor-like)/TIRAP (TIR domain-containing adaptor protein), Trif (TIR-domain-containing adaptor inducing interferon-beta), TRAM (Trif-related adaptor molecule) and SARM (SAM and ARM-containing protein). Different TLRs use different combinations of these adaptors, leading to the activation of common and unique pathways involved in the elimination of the invading microbe.

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Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-κ-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.

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Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases.All members of the family contain SH3 and SH2 domains and, with the exception of Txk and Dsrc28C, also contain a pleckstrin homology (PH) and a Tec homology (TH) domain in their amino termini.BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation.

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is well known as one of the key enzymes involved in glycolysis. It catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains. Besides its functioning as a glycolytic enzyme in cytoplasm, recent evidence suggest that mammalian GAPDH is also involved in a great number of intracellular proceses such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. During the last decade a lot of findings appeared concerning the role of GAPDH in different pathologies including prostate cancer progression, programmed neuronal cell death, age- related neuronal diseases, such as Alzheimer’s and Huntington’s disease.

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HAVCR1, a 359 A.A Class 1 integral membrane glycoprotein, is used by Hepatitis A virus to infect humans. It consists of a conserved N-terminal Cys-rich region, IgV (Immunoglobulin Variable region like) domain and a TSP-rich mucin domain in the extracellular region followed by a highly conserved tyrosine kinase phosphorylation motif in the cytoplasmic region. HAVCR1 is expressed on terminally differentiated CD4+ Th2 cells and regulates cytokine production. It plays an important role in the regulation of immune responses in the development of asthma and allergic responses. Its expression is critically upregulated in dedifferentiated kidney cells, thus indicating a possible role in regeneration of proximal tubule epithelium in Kidneys. HAVCR1 has shown to be upregulated in renal carcinomas, suggesting its role in tumor progression and metastasis.

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FOXA1 Antibody: FOXA1 is one of three members of the FOXA family, a subset of the forkhead family of transcription factors which play vital roles in development. It has also been implicated in the development of a number of other organs including the androgen and estrogen regulated tissues of the breast and prostate. FOXA1 modulates the transcriptional activity of nuclear hormone receptors and regulates apoptosis by inhibiting the expression of BCL-2. It is an essential protein for the transcriptional activity of both androgen receptor (AR) and estrogen receptor-beta (ER). FOXA1 plays a pivotal role from early stage cancer through to drug resistant and metastatic disease. FOXA1 is not only an attractive therapeutic target but could potentially function as a novel biomarker.

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SNCG(also designated gamma-synuclein or breast cancer-specific protein 1),with 127-amino acid protein(about 14 kDa), belongs to the synuclein family, which also includes alpha- and beta- synuclein.Three synucleins are located in the neuronal cytosol and enriched in presynaptic terminals,while SNCG is also expressed in many other non-neuronal tissues. SNCG is abnormally expressed in a high percentage of tumor tissues of diversified cancer types, including liver, esophagus, colon, gastric, lung, prostate, cervical, and breast cancer, but rarely expressed in tumor-matched nonneoplastic adjacent tissues. High levels of SNCG have been identified in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development.

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Glycogen synthase kinase 3 alpha belongs to the Ser/Thr family of protein kinases, Cdc2/cdkx subfamily; GSK3 subsubfamily. It is implicated in the hormonal control of several regulatory proteins including glycogen synthase, myb, and the transcription factor c jun. GSK3 phosphorylates glycogen synthase and thereby inactivates it. Insulin stimulates the dephosphorylation of glycogen synthase at the sites phosphorylated by GSK3 and subsequently inhibits GSK3 acutely leading to the stimulation of glycogen synthesis. GSK3 signaling is performed by two isoforms, GSK3 alpha and GSK3 beta. The two isoforms share 97% sequence similarity within their catalytic domains. GSK3 has also been shown to play a role in protein synthesis, cell adhesion, cell proliferation, cell differentiation, microtubule dynamics and cell motility.

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Glycogen synthase kinase 3 alpha belongs to the Ser/Thr family of protein kinases, Cdc2/cdkx subfamily，GSK3 subsubfamily. It is implicated in the hormonal control of several regulatory proteins including glycogen synthase, myb, and the transcription factor c jun. GSK3 phosphorylates glycogen synthase and thereby inactivates it. Insulin stimulates the dephosphorylation of glycogen synthase at the sites phosphorylated by GSK3 and subsequently inhibits GSK3 acutely leading to the stimulation of glycogen synthesis. GSK3 signaling is performed by two isoforms, GSK3 alpha and GSK3 beta. The two isoforms share 97% sequence similarity within their catalytic domains. GSK3 has also been shown to play a role in protein synthesis, cell adhesion, cell proliferation, cell differentiation, microtubule dynamics and cell motility.

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MER (c-mer proto-oncogene tyrosine kinase) is a member of the MER/AXL/TYRO3 receptor kinase family and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) domains, and one tyrosine kinase domain. MER has been identified as a tyrosine kinase potentially involved in the development of glioblastomas. It is expressed at highest levels in ovary, prostate, lung and kidney. Gas6, a growth arrest specific gene, and the related anticoagulation factor Protein S have been identified as ligands for the UFO family of receptors. Mutations in this gene have been associated with disruption of the retinal pigment epithelium (RPE) phagocytosis pathway and onset of autosomal recessive retinitis pigmentosa (RP).

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SncA is a member of the synuclein family of structurally related proteins that are prominently expressed in the central nervous system, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and SncA and Snc-Beta inhibit phospholipase D2 selectively. SncA may serve to integrate presynaptic signaling and membrane trafficking. Aggregated SncA proteins form brain lesions that are hallmarks of neurodegenerative synucleinopathies. Defects in SncA play a role in the pathogenesis of Parkinson disease. SncA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer disease. SncA shares 95% sequence homology with rat SncA. Rat SncA is specifically expressed in brain and is associated with synaptosomal membranes in neurons

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The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation

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Members in the TNF superfamily regulate immune responses and induce apoptosis. A novel member in the TNF family was recently identified by several groups and designated BAFF (for B cell Activating Factor belonging to the TNF Family), BLyS (for B Lymphocyte Stimulator), TALL-1 (for TNF- and ApoL-related Leukocyte-expressed Ligand), and THANK (for TNF Homologue that Activate Apoptosis, NF-κB and c-jun N-terminal Kinase). BAFF/BLyS was characterized as a B cell activator since it induced B cell proliferation and immunoglobulin secretion. Three receptors for BAFF were recently identified and designated TACI, BCMA and BAFF-R. BAFF and its receptors are essential for B cell development, survival, and humoral immune responses. BAFF is involved in the development of autoimmune diseases including systemic lupus erythaematosus and rheumatoid arthritis.

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General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

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Ractopamine is a phenolethanolamine beta-adrenoceptor agonist that is used for the improvement of weight gain, carcass leanness and feed efficiency in pigs. It has been known for years that ractopamine enhances growth in meat animals by repartitioning nutrients. This means that the nutrients that the animal consumes in its feed are shifted away from being stored as fat and are instead used in lean tissue production. This shift occurs as the animal reaches the top of its growth curve and lean tissue production drops off and fat deposition increases. Fat levels also appear to decrease, due to an increase in lypolysis (fat breakdown). Using the ractopamine monoclonal antibody, it is possible to detect ractopamine and other agonists in urine, muscle and liver both rapidly and with accuracy.

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Rsk1 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 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. RSK proteins possess two separate kinase domains, the C terminal kinase domain and the N terminal kinase domain, separated by a linker region containing a hydrophobic motif. RSK is activated by many stimuli including growth factors, phorbol esters, cAMP, heat shock, and irradiation.