19545 Results for: "Sodium+carbonate+decahydrate"

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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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Baculoviral IAP repeat-containing 5 (survivin).This gene is a member of the inhibitor of apoptosis (IAP) gene family, which encode negative regulatory proteins that prevent apoptotic cell death. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but this gene encodes proteins with only a single BIR domain. The encoded proteins also lack a C-terminus RING finger domain. Gene expression is high during fetal development and in most tumors yet low in adult tissues. Antisense transcripts are involved in the regulation of this gene's expression. At least four transcript variants encoding distinct isoforms have been found for this gene, but the full-length natures of only three of them have been determined.

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NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains. NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma. CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56.

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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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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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MSH2 is a 100 kDa nuclear antigen and encodes a protein of 934 amino acids. The MSH2 gene is one of 4 known genes encoding proteins involved in the repair of mismatch nucleotides following DNA replication or repair. Mutations in the MSH2 gene contribute to the development of sporadic colorectal carcinoma. MSHS mutations are responsible for 50% of inherited non-polyposis colorectal (HNPCC). The repair of mismatch DNA is essential to maintaining the integrity of genetic information over time. An alteration of microsatellite repeats is the result of slippage owing to strand misalignment during DNA replication and is referred to as microsatellite instability (MSI). These defects in DNA repair pathways have been related to human carcinogenesis. MSH-2 is involved in the initial cognition of mismatch nucleotides during the replication mismatch repair process.

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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抯 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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The Itg-Beta3 gene encodes the beta subunit of the platelet membrane adhesive protein receptor complex Itg-Beta3 protein, which belongs to the Integrin class of cell adhesion molecule receptors that share a common heterotrimeric structure with Alpha and Beta subunits. It is a common Beta subunit of the platelet complex and of two other Integrins (Fibronectin and Vitronectin Receptors), which have distinct Alpha subunits. Itg-Beta3 has been implicated in a wide variety of functions, including platelet aggregation and thrombosis and implantation, placentation, angiogenesis, bone remodeling, and tumor progression. Glanzmann Thrombasthenia can result from defects in the genes for either the Itg-Alpha2B or the Itg-Beta3 subunit

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Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.

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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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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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Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2, 6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

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IL-36G is is a member of the interleukin 1 cytokine family whose gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. IL-36G is thought to activate the NF-kappaB pathway through IL-1 receptor family members IL-1RL2 and IL-1RAcP. Like the related proteins IL-36A and IL-36B, IL-36G requires post-translational processing for full agonist activity, but the cleavage mechanism is currently unknown. IL-36G expression is stimulated by interferon-gamma, tumor necrosis factor-alpha and interleukin 1. The IL-36 cytokines have been suggested to amplify Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells.

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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