27728 Results for: "affinity chromatography"

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Galactocerebrosides are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system and are also present in small amounts in kidney. The key enzymatic step in the biosynthesis of galactocerebrosides consists of the transfer of galactose to ceramide catalyzed by UDP-galactose ceramide galactosyltransferase (CGT, EC 2.4.1.45). The enzyme UGT8 is the first involved in complex lipid biosynthesis in the myelinating oligodendrocyte.Galactocerebrosides are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system and are also present in small amounts in kidney. The key enzymatic step in the biosynthesis of galactocerebrosides consists of the transfer of galactose to ceramide catalyzed by UDP-galactose ceramide galactosyltransferase (CGT, EC 2.4.1.45). The enzyme encoded by the CGT gene is the first involved in complex lipid biosynthesis in the myelinating oligodendrocyte.

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TRIM8 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to nuclear bodies. Its structure is similar to some tumor suppressor proteins and its gene maps to a locus thought to contain tumor suppressor genes.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to nuclear bodies. Its structure is similar to some tumor suppressor proteins and its gene maps to a locus thought to contain tumor suppressor genes.

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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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ATF4 encodes a transcription factor that was originally identified as a widely expressed mammalian DNA bindingprotein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB-2). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP-1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein-protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA binding domain. Two alternative transcripts encoding the same protein have been described. Two pseudogenes are located on the X chromsome at q28 in a region containing a large inverted duplication.

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VAX1 is a homeo-domain containing protein from a class of homeobox transcription factors which are conserved in vertebrates. It may play an important role in the development of anterior ventral forebrain and visual system.This gene encodes a homeo-domain containing protein from a class of homeobox transcription factors which are conserved in vertebrates. Genes of this family are involved in the regulation of body development and morphogenesis. The most conserved genes, called HOX genes are found in special gene clusters. This gene belongs to the VAX subfamily and lies in the vicinity of the EMX homeobox gene family. Another member of VAX family is located on chromosome 2. The encoded protein may play an important role in the development of anterior ventral forebrain and visual system. Multiple transcript variants encoding different isoforms have been found for this gene.

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TSPAN6 is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This protein is a cell surface glycoprotein and is highly similar in sequence to the transmembrane 4 superfamily member 2. The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein and is highly similar in sequence to the transmembrane 4 superfamily member 2. The use of alternate polyadenylation sites has been found for this gene.

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ST8SIA2 is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. ST8SIA2 may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.

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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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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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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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Human IL13 was originally identified by differential screening of an anti CD28 activated human peripheral blood mononuclear cell cDNA library as an induction specific novel cytokine. It was also isolated from cDNA libraries of human T cell clones using the murine IL13 (P600) cDNA as a probe. Human IL13, a pleiotropic cytokine, is produced by activated Th0, Th1 like, Th2 like, and CD8 T cells. The gene for human IL13 maps to chromosome 5 and is closely linked to the genes for IL3, IL4, IL5, and GMCSF.

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Interleukin 11 is a pleiotropic cytokine produced by mesenchymal-derived adherent cells. IL11 shares many functions of IL6 and LIF, including potentiation of megakaryocyte activity, enhancement of human myeloma cell proliferation, and enhancement of hepatic acute phase protein production. Interleukin 11 directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation resulting in increased platelet production. Clinically it is used to prevent severe thrombocytopenia and the reduction of the need for platelet transfusion following myelosuppressive chemotherapy.

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PPP1R13B is a member of the ASPP (apoptosis-stimulating protein of p53) family of p53 interacting proteins. The protein contains four ankyrin repeats and an SH3 domain involved in protein-protein interactions. ASPP proteins are required for the induction of apoptosis by p53-family proteins. They promote DNA binding and transactivation of p53-family proteins on the promoters of proapoptotic genes. Expression of this gene is regulated by the E2F transcription factor.This gene encodes a member of the ASPP (apoptosis-stimulating protein of p53) family of p53 interacting proteins. The protein contains four ankyrin repeats and an SH3 domain involved in protein-protein interactions. ASPP proteins are required for the induction of apoptosis by p53-family proteins. They promote DNA binding and transactivation of p53-family proteins on the promoters of proapoptotic genes. Expression of this gene is regulated by the E2F transcription factor.

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ZNF322 contains four exons and spans 23.2kb in chromosome 6p22.1 region, and transcribes a 2.7kb mRNA that encodes a protein with 402 amino acid residues.Through northern blot analysis, ZNF322 was shown to be expressed in every human tissue examined at adult stage and during embryonic developmental stages from 80 days to 24 weeks. When ZNF322 was overexpressed in COS-7 cells, ZNF322-EGFP fusion protein is detected in the nucleus and cytoplasm. Reporter gene assays show that ZNF322 is a transcriptional activator. Furthermore, overexpression of ZNF322 in COS-7 cells activates the transcriptional activity of SRE and AP-1. Together, these results suggest that ZNF322 is a member of the zinc-finger transcription factor family and may act as a positive regulator in gene transcription mediated by the MAPK signaling pathways.

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Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP18 is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This protein directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression when tethered to the promoter.Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This protein directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression when tethered to the promoter.

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HTATIP belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction.The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction. Alternative splicing of this gene results in multiple transcript variants.

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Cyclin-dependent kinase activity is regulated by T-loop phosphorylation (Thr172 in the case of CDK4), by the abundance of their cyclin partners, and by association with CDK inhibitors of the Cip/Kip or INK family of proteins. The inactive ternary complex of CDK4/cyclin D and p27 Kip1/Cip1 requires extracellular mitogenic stimuli for the release and degradation of p27, which affects progression through the restriction point and pRb-dependent entry into S-phase. The active complex of CDK4/cyclin D targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression. In HeLa cells, upon UV irradiation, upregulation of p16 INK4A association with CDK4/cyclin D3 leads to a G2 delay, implicating CDK4/cyclin D3 activity in progression through the G2-phase of the cell cycle.

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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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Macrophage Inflammatory Protein 1 alpha and MIP1 beta, two closely related but distinct proteins, were originally co-purified from medium conditioned by a LPS-stimulated murine macrophage cell line. Mature mouse MIP1 alpha shares approximately 77% and 70% amino acid identity with human MIP1 alpha and mouse MIP1 beta, respectively. MIP1 proteins are expressed primarily in T cells, B cells, and monocytes after antigen or mitogen stimulation.

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ST3GAL2 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.

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Members of the SOX family of transcription factors are characterized by the presence of a DNA-binding high mobility group (HMG) domain, homologous to the HMG box of sex-determining region Y (SRY). Forming a subgroup of the HMG domain superfamily, SOX proteins have been implicated in cell fate decisions in a diverse range of developmental processes. SOX transcription factors have diverse tissue-specific expression patterns during early development and have been proposed to act as target-specific transcription factors and/or as chromatin structure regulatory elements. The SOX12 gene encodes a protein that was identified as a SOX family member based on conserved domains and its expression in various tissues suggests a role in both differentiation and maintenance of several cell types.

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HR is a protein whose function has been linked to hair growth. A similar protein in rat functions as a transcriptional corepressor for thyroid hormone and interacts with histone deacetylases. Mutations in this gene have been documented in cases of autosomal recessive congenital alopecia and atrichia with papular lesions.This gene encodes a protein whose function has been linked to hair growth. A similar protein in rat functions as a transcriptional corepressor for thyroid hormone and interacts with histone deacetylases. Mutations in this gene have been documented in cases of autosomal recessive congenital alopecia and atrichia with papular lesions. Two transcript variants encoding different isoforms have been found for this gene.

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GALNAC4S-6ST is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc (4,6-SO (4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc (4SO4)-GlcA (2SO4)-GalNAc (6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. GALNAC4S-6ST may also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo.

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N-alpha-acetylation is one of the most common protein modifications that occurs during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino group. ARD1A, together with NATH (NARG1; MIM 608000), is part of a major N-alpha-acetyltransferase complex responsible for alpha-acetylation of proteins and peptides.N-alpha-acetylation is one of the most common protein modifications that occurs during protein synthesis and involves the transfer of an acetyl group from acetyl-coenzyme A to the protein alpha-amino group. ARD1A, together with NATH (NARG1; MIM 608000), is part of a major N-alpha-acetyltransferase complex responsible for alpha-acetylation of proteins and peptides (Sanchez-Puig and Fersht, 2006 [PubMed 16823041]).

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TSPAN3 is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. The use of alternate polyadenylation sites has been found for this gene. Two alternative transcripts encoding different isoforms have been described.

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Interleukin-22 (IL-22) is a cytokine important for the modulation of tissue responses during inflammation. Unlike the distantly related IL-10, IL-22 does not inhibit the production of proinflammatory cytokines in monocytes in response to LPS, but it has some inhibitory effects on IL-4 production from Th2 T cells. IL-22 is expressed by both the adaptive arm of the immune system such as CD4 T cell subsets including Th17 cells, as well as by innate lymphocytes such as NK and LTi-like cells. IL-22 is highly expressed in several chronic inflammatory conditions, and studies suggest that IL-22 plays both inflammatory and protective roles.

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IL-9 is a cytokine preferentially produced by T helper type 2 lymphocytes and active on various cell types such as T and B lymphocytes, mast cells and haemopoietic progenitors; but no effect of this cytokine has been reported so far on mononuclear phagocytes. IL-9 stimulates cell proliferation and prevents apoptosis. The IL-9 receptor (IL 9R) belongs to the haemopoietic receptor superfamily and its signal transduction involves mainly the (JAK/STAT) pathway. Some studies have implicated IL-9 as an important cytokine in a number of Th2 cytokine mediated pathologies, in particular asthma

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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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RANTES is a chemoattractant for blood monocytes, memory T helper cells and eosinophils. It causes the release of histamine from basophils and activates eosinophils. It binds to CCR1, CCR3, CCR4 and CCR5 and is one of the major HIV suppressive factors produced by CD8+ T cells. Recombinant RANTES protein induces a dose dependent inhibition of different strains of HIV 1, HIV 2, and simian immunodeficiency virus (SIV). It is T cell and macrophage specific, induced by mitogens, and belongs to the intercrine beta (chemokine CC) family.

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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