25813 Results for: "affinity chromatography"

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NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 or IKBKB, MIM 603258) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).

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PDGF Receptor beta encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. This gene is flanked on chromosome 5 by the genes for granulocyte-macrophage colony-stimulating factor and macrophage-colony stimulating factor receptor; all three genes may be implicated in the 5-q syndrome. A translocation between chromosomes 5 and 12, that fuses this gene to that of the translocation, ETV6, leukemia gene, results in chronic myeloproliferative disorder with eosinophilia.

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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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RHBDL2 is a member of the rhomboid family of integral membrane proteins. This family contains proteins that are related to Drosophila rhomboid protein. Members of this family are found in both prokaryotes and eukaryotes and are thought to function as intramembrane serine proteases. RHBDL2 is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3.The protein encoded by this gene is a member of the rhomboid family of integral membrane proteins. This family contains proteins that are related to Drosophila rhomboid protein. Members of this family are found in both prokaryotes and eukaryotes and are thought to function as intramembrane serine proteases. The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3.

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Nanog is a newly identified homeodomain-bearing transcriptional factor. Nanog expression is specific to early embryos and pluripotential stem cells including mouse and human embryonic stem (ES) and embryonic germ (EG) cells. It is a key molecule involved in the signaling pathway for maintaining the capacity for self-renewal and pluripotency, bypassing regulation by the STAT3 pathway. Nanog mRNA is present in pluripotent mouse and human cell lines, and absent from differentiated cells. Nanog-deficient ES cells lose pluripotency and differentiate into extraembryonic endoderm lineage. Thus it is one of the molecular markers suitable for recognizing the undifferentiated state of stem cells in the mouse and human.

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Interleukin 2 (IL2) is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli. IL2 has been shown to have antitumor effects in some studies. This is probably mediated by cytotoxic effector cells.

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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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CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. TRDMT1 is a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome.CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome. Alternative splicing results in multiple transcript variants encoding different isoforms.

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FKBP8 is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. Unlike the other members of the family, it does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function.The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. Unlike the other members of the family, this encoded protein does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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The protein encoded by TRIM68 contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. TRIM68 is expressed in many cancer cell lines. Its expression in normal tissues, however, was found to be restricted to prostate. TRIM68 was also found to be differentially expressed in androgen-dependent versus androgen-independent prostate cancer cells. The protein encoded by this gene contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. This gene is expressed in many cancer cell lines. Its expression in normal tissues, however, was found to be restricted to prostate. This gene was also found to be differentially expressed in androgen-dependent versus androgen-independent prostate cancer cells.

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ENO3 is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in skeletal muscle cells in the adult. A switch from alpha enolase to beta enolase occurs in muscle tissue during development in rodents. Mutations in ENO3 gene can be associated with metabolic myopathies that may result from decreased stability of the enzyme.This gene encodes one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in skeletal muscle cells in the adult. A switch from alpha enolase to beta enolase occurs in muscle tissue during development in rodents. Mutations in this gene can be associated with metabolic myopathies that may result from decreased stability of the enzyme. Two transcripts have been identified for this gene that differ only in their 5' UTR.

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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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PRDX6 is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H (2)O (2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H (2)O (2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism and transport of nuclear pre-mRNA transcripts. hnRNP A1 regulates the alternative splicing of c-Src, c-H-Ras and modifies initiation of translation of the fibroblast growth factor 2 mRNA. hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells. Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus. hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production. HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm ,

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Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.

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IL-15 (14-15 kD) is a member of the four alpha-helical bundle family of cytokines. It is very similar to IL-2, except that IL-15 has an IL-15 alpha receptor subunit. IL-15 plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules. This implies that IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases.

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NCKAP1L is a member of the HEM family of tissue-specific transmembrane proteins which are highly conserved from invertebrates through mammals. This gene is only expressed in hematopoietic cells, while hematopoietic protein 2 is preferentially expressed in brain, heart, liver and testis. The function of the HEM1 product has not been established but it is thought to play an essential role in oogenesis.The protein encoded by this gene is a member of the HEM family of tissue-specific transmembrane proteins which are highly conserved from invertebrates through mammals. This gene is only expressed in hematopoietic cells, while hematopoietic protein 2 is preferentially expressed in brain, heart, liver and testis. The function of the HEM1 product has not been established but it is thought to play an essential role in oogenesis.

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Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms. This enzyme is required for embryonic development since TH knockout mice die before or at birth. Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH. Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels.

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EEF1G is a subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This subunit contains an N-terminal glutathione transferase domain, which may be involved in regulating the assembly of multisubunit complexes containing this elongation factor and aminoacyl-tRNA synthetases.This gene encodes a subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This subunit contains an N-terminal glutathione transferase domain, which may be involved in regulating the assembly of multisubunit complexes containing this elongation factor and aminoacyl-tRNA synthetases. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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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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ST8SIA4 catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). ST8SIA4, a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus.The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.

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ApoM(apolipoprotein M,also designated G3a or NG20),with 188-amino acid protein(about 21 kDa),is an apolipoprotein and member of the lipocalin protein family.The Apo-proteins are involved in the specific binding of cellular receptors, the regulation of lipolytic enzymes, and the process of lipid exchange. The encoded protein is secreted through the plasma membrane but remains membrane-bound, where it is involved in lipid transport.The N-terminal region of Apo-M contains hydrophobic residues that may promote association with the phospholipid layer of lipoprotein particles. In vitro,Apo-M is glycosylated when translated in the presence of microsomes, and remains associated with the microsomes after carbonate treatment.Apo-M is expressed in liver and kidney, and is secreted into the bloodstream in HDLs,and also found in triglyceride-rich lipoproteins and LDLs.

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Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation. Mediates MYC-mediated let-7 repression. Isoform 1, when overexpressed, stimulates growth of the breast adenocarcinoma cell line MCF-7. Isoform 2 has no effect on cell growth.

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RRAS2 Antibody: Activating mutations and overexpression of classical Ras subfamily members (K-RAS, N-RAS and H-RAS) have been widely investigated as key events in the development of human cancers. The RRAS subfamily of Ras-related proteins includes RRAS1, RRAS2 (TC21) and RRAS3 (M-Ras) show overall amino acid identity with the classical Ras subfamily (H-Ras, K-Ras and N-Ras) of 55–60%. RRAS2 is a small GTPbinding protein of the Ras superfamily of GTPases. It might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins. RRAS2 has high oncogenic potential and overexpression/mutations have been reported in several tumor tissues and cell lines.

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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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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 PAX5 gene is a member of the paired box (PAX) family of transcription factors. The central feature of this gene family is a novel, highly conserved DNA-binding motif, known as the paired box. The PAX proteins are important regulators in early development, and alterations in the expression of their genes are thought to contribute to neoplastic transformation. The PAX5 gene encodes the B-cell lineage specific activator protein (BSAP) that is expressed at early, but not late stages of B-cell differentiation. Its expression has also been detected in developing CNS and testis, therefore, PAX5 gene product may not only play an important role in B-cell differentiation, but also in neural development and spermatogenesis.

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TNFSF4 Antibody: The tumor necrosis factor superfamily member TNFSF4 is a type II membrane bound, non-covalently linked homotrimeric protein. It is expressed on antigen presenting cells, such as dendritic cells and activated B-cells, and also on other cells such as vascular endothelial cells, mast cells, and natural killer cells. TNFSF4 signals specifically through the TNFRSF4 receptor, is expressed predominantly on CD4+T cells but also on certain activated CD8+T cells. TNFRSF4/TNFSF4 functions as a costimulatory signal, which is required for a productive interaction between antigen presenting cells and their target T-cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNgamma. TNFRSF4/TNFSF4 signaling plays an important role in immunotolerance.

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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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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