17294 Results for: "Sodium+hydrogen-L-tartrate"

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Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.

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Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter (reviewed in 1). Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase (2). Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle (3). Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.

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AminoLink™ Plus Coupling Resin uses aldehyde-activated agarose beads for high-yield covalent coupling of antibodies (proteins) via primary amines to prepare columns for affinity purification.

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CCNT1 Antibody: Cyclins function as regulators of CDK kinases and exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. The cyclin-T1 protein (CCNT1) belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. CCNT1 tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing CCNT1 and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. CCNT1 and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.

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S-Monovette® is a blood collection system that combines two blood collection techniques – aspiration and vacuum. The S-Monovette® is suitable for all vein conditions and achieves an optimal sample quality, thereby producing the best results. The aspiration technique is a gentle technique for routine blood collection. Using the vacuum technique, a "fresh" vacuum is always available.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

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FES (feline sarcoma oncogene) and Fer are the only two members of a unique family of cytoplasmic protein tyrosine kinases. FES and Fer contain a central Src homology-2 (SH2) domain and a carboxy-terminal tyrosine kinase catalytic domain. They are structurally distinguished from other members of cytoplasmic protein tyrosine kinase subfamilies by the presence of amino-terminal Fer/CIP4 homology and coiled-coil domains. FES was originally identified as an oncogene from avian and feline retroviruses. Human c-Fes has been implicated in myeloid, vascular endothelial and neuronal cell differentiation. FES has tyrosine-specific protein kinase activity and that activity is required for maintenance of cellular transformation. Mutations may activate the FES kinase and thereby contribute to cancer. However, recent data strongly suggests that the c-FES protein-tyrosine kinase is a tumor suppressor rather than a dominant oncogene in colorectal cancer.

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The progression of cells through the cell cycle is regulated by a family of protein kinases known as cyclin-dependent kinases (Cdks). The sequential activation of individual members of this family and their consequent phosphorylation of critical substrates promotes orderly progression through the cell cycle. The cyclins function as differentially expressed positive regulators of Cdks. Negative regulators of the cycle include the p53-inducible 21 kDa WAF1/Cip1 protein designated p21, Kip1 p27 and p16. The complexes formed by Cdk4 and the D-type cyclins have been strongly implicated in the control of cell proliferation during the G1 phase. It has recently been shown that p16 binds to Cdk4 and inhibits the catalytic activity of the Cdk4/cyclin D complex. Moreover, the gene encoding p16 exhibits a high frequency of homozygous deletions and point mutations in established human tumor cell lines.

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CK5 (keratin 5) is a member of the keratin gene family. Biochemically, most members of the CK family fall into one of two classes, type I (acidic polypeptides) and type II (basic polypeptides). The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. This type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. At least one member of the acidic family and one member of the basic family is expressed in all epithelial cells. Cytokeratin 5 is expressed in normal basal cells. Mutations of the Cytokeratin5 gene (KRT5) have been shown to result in the autosomal dominant disorderepidermolysis bullosa (EB). Defects in KRT5 are a cause of epidermolysis bullosa simplex.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

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The progression of cells through the cell cycle is regulated by a family of protein kinases known as cyclin-dependent kinases (Cdks). The sequential activation of individual members of this family and their consequent phosphorylation of critical substrates promotes orderly progression through the cell cycle. The cyclins function as differentially expressed positive regulators of Cdks. Negative regulators of the cycle include the p53-inducible 21 kDa WAF1/Cip1 protein designated p21, Kip1 p27 and p16. The complexes formed by Cdk4 and the D-type cyclins have been strongly implicated in the control of cell proliferation during the G1 phase. It has recently been shown that p16 binds to Cdk4 and inhibits the catalytic activity of the Cdk4/cyclin D complex. Moreover, the gene encoding p16 exhibits a high frequency of homozygous deletions and point mutations in established human tumor cell lines.

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This gene encodes a multifunctional protein that is involved in various cellular processes, including gene expression, cell signaling, and RNA processing and transport. The protein includes an N-terminal transcriptional activation domain and a C-terminal RNA-binding domain. Chromosomal translocations between this gene and various genes encoding transcription factors result in the production of chimeric proteins that are involved in tumorigenesis. These chimeric proteins usually consist of the N-terminal transcriptional activation domain of this protein fused to the C-terminal DNA-binding domain of the transcription factor protein. Mutations in this gene, specifically a t(11;22)(q24;q12) translocation, are known to cause Ewing sarcoma as well as neuroectodermal and various other tumors. Alternative splicing of this gene results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 1 and 14.

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Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of the Polycomb group (PcG) multiprotein PRC1 complex, a complex required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex act via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity.

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RIP1 Antibody: RIP1 (Receptor Interacting Protein), also known as RIPK1, is a crucial 74 kD adaptor kinase in several of stress-induced signaling pathways and on the crossroad of a cell’s decision to live or die. RIP1 contains an N-terminal region with homology to protein kinases, an intermediate domain capable of association with MAPKKK and a C-terminal region containing a death domain motif present in the Fas and TNFR1 intracellular domains. Full length RIP1 is important for signallling to NF-kappa-B, MAPKs and necrosis, whereas caspase-8 generates a C-terminal RIP1 cleavage fragment, promoting TNF-induced apoptosis. It is required for TNFRSF1A-mediated and TLR3-induced NF-kappa-B activation. RIP1-deficient mice fail to thrive, displaying extensive apoptosis in both lymphoid and adipose tissues and dying at 1-3 days of age.

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This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. When present in a hybrid receptor with INSR, binds IGF1. Ref.19 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, Ref.21 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.

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S100B (S100 calcium binding protein B) is a member of the S100 family of proteins containing 2 EF-hand calcium binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S-100 proteins and parvalbumin proteins are each expressed in neural tissues. In addition, S100B are present in a variety of other tissues, and calbindin is present in intestine and kidney. Parvalbumin B is found in many tumor tissues as well as in the organ of Corti. Calbindin, S-100 proteins and parvalbulmins have all been detected in leydig cells and the testis. These proteins are thought to play a role in hormone production and spermatogenesis. Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

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The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation.

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Signaling adapter that couples activated growth factor receptors to signaling pathway. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span

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A family of protein kinases located upstream of the MAP kinases andresponsible for their activation has been identified. The prototype member ofthis family, designated MAP kinase kinase, or MEK-1, specifically phospho-rylates the MAP kinase regulatory threonine and tyrosine residues present inthe Thr-Glu-Tyr motif of ERK. A second MEK family member, MEK-2, resem-bles MEK-1 in its substrate specificity. MEK-3 (or MKK-3) functions to acti-vate p38 MAP kinase, and MEK-4 (also called SEK1 or MKK-4) activatesboth p38 and JNK MAP kinases. MEK-5 appears to specifically phosphory-late ERK5, whereas MEK-6 phosphorylates p38 and p38b. MEK-7 (or MKK-7)phosphorylates and activates the JNK signal transduction pathway.

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B-raf Antibody: B-raf belongs to the raf/mil family of serine/threonine protein kinases and plays a role in regulating the MAP kinase/ERKs signaling pathway, which affects cell division, differentiation, and secretion. The Ras/Raf/MEK/ERK and Ras/PI3K/PTEN/Akt pathways interact with each other to regulate growth and in some cases tumorigenesis. Mutations in B-raf have been associated with several cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, and adenocarcinoma of lung, leading to speculation on the possibility of B-raf as a therapeutic target for treating cancers. Mutations in this gene have also been associated with cardiofaciocutaneous syndrome (CFCS), a disease characterized by heart defects, mental retardation and a distinctive facial appearance.

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Kaposi's sarcoma-associated herpesvirus (KSHV) belongs to the gamma-(2)-herpesvirus subfamily and has been closely linked to the Kaposi’s sarcoma, primary effusion lymphoma (PEL) and multicentric Castleman’s disease. The genome of KSHV is 165-170 kb and contains at least 88 open reading frames. At least five major proteins are likely to be involved in the assembly of the HHV-8 capsid, including a protease (encoded by ORF17), the major capsid protein (encoded by ORF25), and three other smaller capsid proteins (encoded by ORF62, ORF26, and ORF65). Previous structural studies have shown that the HSV-1 triplex is a monomer of VP19c and a dimer of VP23 and that the HCMV triplex is similarly composed of a monomer and a dimer. By analogy, the KSHV triplexes are likely also composed of a monomer of the ORF62 protein and a dimer of the ORF26 protein, which are the respective homologs of VP19c and VP23.

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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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STAT6 is a member of the STAT family of transcription factors. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor-associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. By screening an embryonic lung fibroblast cDNA library with a wildtype STAT6 probe, 2 variant cDNAs were identified, which were termed STAT6B and STAT6C, encoding an N-terminal 110-amino acid truncation and a 27-amino acid deletion in the SH2 domain, respectively. All the three variants are ubiquitously expressed with STAT6B expression greatest in spleen and STAT6C expression greatest in lung. STAT6B resembles an attenuated STAT6, but that STAT6C inhibits IL-4-mediated mitogenesis and cell surface antigen expression, and is not tyrosine phosphorylated

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Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

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IGF1R(insulin-like growth factor 1 receptor), a transmembrane receptor tyrosine kinase, is widely expressed in many cell types within fetal and postnatal tissues, and in many cell lines. Upon binding to its ligands, IGF-I and IGF-II, receptor autophosphorylation occurs. The triple tyrosine cluster within the kinase domain (Tyr1131, Tyr1135 and Tyr1136) is the earliest major site of autophosphorylation. Phosphorylation of these three tyrosine residues is necessary for kinase activation.Insulin receptors (IRs) share significant similarity with IGF1 receptors in both structure and function,including an equivalent triple tyrosine cluster within the activation loop of the kinase domain (Tyr1146, Tyr1150 and Tyr1151).Tyrosine autophosphorylation of insulin receptor is one of the earliest cellular responses to insulin stimulation. Autophosphorylation begins with phosphorylation of Tyr1146 and either Tyr1150 or Tyr1151. Full kinase activation requires the triple tyrosine phosphorylation.

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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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This gene is a target gene of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of this gene can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. More than 40 different alternatively spliced transcript variants have been isolated from both tumor and normal tissues

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Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.