35955 Results for: "tbe+buffer"

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RBPJL is similar in sequence to the mouse RPB-L protein and Drosophila suppressor of hairless protein. In mouse, recombining binding protein L (RBP-L) is a transcription factor that binds to DNA sequences almost identical to that bound by the Notch receptor signalling pathway transcription factor RBP-J. However, unlike RBP-J, RBP-L does not interact with Notch receptors. RBP-L has been shown to activate transcription in concert with Epstein-Barr virus nuclear antigen-2 (EBNA2). RBPJL is similar in sequence to the mouse RPB-L protein and Drosophila suppressor of hairless protein.In mouse, recombining binding protein L (RBP-L) is a transcription factor that binds to DNA sequences almost identical to that bound by the Notch receptor signalling pathway transcription factor RBP-J. However, unlike RBP-J, RBP-L does not interact with Notch receptors. RBP-L has been shown to activate transcription in concert with Epstein-Barr virus nuclear antigen-2 (EBNA2). The protein encoded by this gene is similar in sequence to the mouse RPB-L protein and Drosophila suppressor of hairless protein.

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At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. GSTM2 is a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione.Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs.

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C1QB is a major constituent of the human complement subcomponent C1q. C1q associates with C1r and C1s in order to yield the first component of the serum complement system. Deficiency of C1q has been associated with lupus erythematosus and glomerulonephritis. C1q is composed of 18 polypeptide chains: six A-chains, six B-chains, and six C-chains. Each chain contains a collagen-like region located near the N terminus and a C-terminal globular region. The A-, B-, and C-chains are arranged in the order A-C-B on chromosome 1. C1QB is the B-chain polypeptide of human complement subcomponent C1q.This gene encodes a major constituent of the human complement subcomponent C1q. C1q associates with C1r and C1s in order to yield the first component of the serum complement system. Deficiency of C1q has been associated with lupus erythematosus and glomerulonephritis. C1q is composed of 18 polypeptide chains: six A-chains, six B-chains, and six C-chains. Each chain contains a collagen-like region located near the N terminus and a C-terminal globular region. The A-, B-, and C-chains are arranged in the order A-C-B on chromosome 1. This gene encodes the B-chain polypeptide of human complement subcomponent C1q.

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NR1I2 belongs to the nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. NR1I2 contains a zinc finger domain.NR1I2 is a transcriptional regulator of the cytochrome P450 gene CYP3A4, binding to the response element of the CYP3A4 promoter as a heterodimer with the 9-cis retinoic acid receptor RXR. It is activated by a range of compounds that induce CYP3A4, including dexamethasone and rifampicin. The gene product belongs to the nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. The encoded protein is a transcriptional regulator of the cytochrome P450 gene CYP3A4, binding to the response element of the CYP3A4 promoter as a heterodimer with the 9-cis retinoic acid receptor RXR. It is activated by a range of compounds that induce CYP3A4, including dexamethasone and rifampicin. The gene product contains a zinc finger domain. Three alternatively spliced transcripts that encode different isoforms have been described, one of which encodes two products through the use of alternative translation initiation codons. Additional transcript variants derived from alternative promoter usage, alternative splicing, and/or alternative polyadenylation exist, but they have not been fully described.

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Homeobox-containing genes are thought to have a role in controlling development. In Drosophila, the 'engrailed' (en) gene plays an important role during development in segmentation, where it is required for the formation of posterior compartments. Different mutations in the mouse homologs, En1 and En2, produced different developmental defects that frequently are lethal. The human engrailed homologs 1 and 2 encode homeodomain-containing proteins and have been implicated in the control of pattern formation during development of the central nervous system.Homeobox-containing genes are thought to have a role in controlling development. In Drosophila, the 'engrailed' (en) gene plays an important role during development in segmentation, where it is required for the formation of posterior compartments. Different mutations in the mouse homologs, En1 and En2, produced different developmental defects that frequently are lethal. The human engrailed homologs 1 and 2 encode homeodomain-containing proteins and have been implicated in the control of pattern formation during development of the central nervous system. 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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Recognizes a 47-55kDa-tumor suppressor protein, identified as Wilm's Tumor (WT1) protein. The antibody reacts with all isoforms of the full-length WT1 and also identifies WT1 lacking exon 2-encoded amino acids, frequently found in subsets of sporadic Wilm s tumors. WT1, a sporadic and familial pediatric kidney tumor, is genetically heterogeneous. Wilm s tumor is associated with mutations of WT1, a zinc-finger transcription factor that is essential for the development of the metanephric kidney and the urogenital system. The WT1 gene is normally expressed in fetal kidney and mesothelium, and its expression has been suggested as a marker for Wilm s tumor and mesothelioma. WT1 protein has been identified in proliferative mesothelial cells, malignant mesothelioma, ovarian carcinoma, gonadoblastoma, nephroblastoma, and desmoplastic small round cell tumor. Lung adenocarcinomas rarely stain positive with this antibody. WT1 protein expression in mesothelial cells has become a reliable marker for the diagnosis of mesotheliomas.

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The antibody HEB-29 reacts with human blood group B. The specificity of the antibody HEB-29 was confirmed by comparison of specificity and reactivity to standard reagent using >5.000 samples of blood. mAb HEB-29 shows specific staining of erythrocytes and vascular epithelium of blood group B controls and no staining in group A controls. It is applicable for tissue staining in tumor patients with blood groups B and AB. Blood group antigens are generally defined as molecules formed by sequential addition of saccharides to the carbohydrate side chains of lipids and proteins detected on erythrocytes and certain epithelial cells. The A, B and H antigens are reported to undergo modulation during malignant cellular transformation. Blood group related antigens represent a group of carbohydrate determinants carried on both glycolipids and glycoproteins. They are usually mucin type, and are detected on erythrocytes, certain epithelial cells, and in secretions of certain individuals. Sixteen genetically and biosynthetically distinct but inter related specificities belong to this group of antigens, including A, B, H, Lewis A, Lewis B, Lewis X, Lewis Y, and precursor type 1 chain antigens.

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Recognizes a sialoglycoprotein of 27-32kDa, identified as CD99, or MIC2 gene product, or E2 antigen. MIC2 gene is located in the pseudo-autosomal region of the human X and Y chromosome. MIC2 gene encodes two distinct proteins, which are produced by alternative splicing of the CD99 gene transcript and are identified as bands of 30 and 32kDa (p30/32). Although its function is not fully understood, CD99 is implicated in various cellular processes including homotypic aggregation of T cells, upregulation of T cell receptor and MHS molecules, apoptosis of immature thymocytes and leukocyte diapedesis. CD99 is expressed on the cell membrane of some lymphocytes, cortical thymocytes, and granulosa cells of the ovary. Most pancreatic islet cells, Sertoli cells of the testis, and some endothelial cells express this antigen. Mature granulocytes express very little or no CD99. MIC2 is strongly expressed on Ewing s sarcoma cells and primitive peripheral neuroectodermal tumors.

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This antibody recognizes proteins of 80-200kDa, identified as different members of the CEA (Carcinoembryonic Antigen) family. CEA is synthesized during development in the fetal gut and is re-expressed in increased amounts in intestinal carcinomas and several other tumors. This antibody does not react with nonspecific cross-reacting antigen (NCA) and with human polymorphonuclear leucocytes. The antibody shows no reaction with a variety of normal tissues and is suitable for staining of formalin/paraffin tissues. CEA is not found in benign glands, stroma, or malignant prostatic cells. antibody to CEA is useful in detecting early foci of gastric carcinoma and in distinguishing pulmonary adenocarcinomas (60-70% are CEA+) from pleural mesotheliomas (rarely or weakly CEA+). CEA antibody positivity is seen in adenocarcinomas from the lung, colon, stomach, esophagus, pancreas, gallbadder, urachus, salivary gland, ovary, and endocervix.

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RAD18 is highly similar to S. cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions through its interaction with Rad6, which is an ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Similar to its yeast counterpart, RAD18 is able to interact with the human homolog of yeast Rad6 protein through a conserved ring-finger motif. Mutation of this motif results in defective replication of UV-damaged DNA and hypersensitivity to multiple mutagens. The protein encoded by this gene is highly similar to S. cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions through its interaction with Rad6, which is an ubiquitin-conjugating enzyme required for post-replication repair of damaged DNA. Similar to its yeast counterpart, this protein is able to interact with the human homolog of yeast Rad6 protein through a conserved ring-finger motif. Mutation of this motif results in defective replication of UV-damaged DNA and hypersensitivity to multiple mutagens. 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMA1 is a member of the peptidase T1A family which is a 20S core alpha subunit.The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified.

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Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures.Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H1 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6. 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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ING3 is similar to ING1, a tumor suppressor protein that can interact with TP53, inhibit cell growth, and induce apoptosis. This protein contains a PHD-finger, which is a common motif in proteins involved in chromatin remodeling. This gene can activate p53 trans-activated promoters, including promoters of p21/waf1 and bax. Overexpression of this gene has been shown to inhibit cell growth and induce apoptosis. Allelic loss and reduced expression of this gene were detected in head and neck cancers.The protein encoded by this gene is similar to ING1, a tumor suppressor protein that can interact with TP53, inhibit cell growth, and induce apoptosis. This protein contains a PHD-finger, which is a common motif in proteins involved in chromatin remodeling. This gene can activate p53 trans-activated promoters, including promoters of p21/waf1 and bax. Overexpression of this gene has been shown to inhibit cell growth and induce apoptosis. Allelic loss and reduced expression of this gene were detected in head and neck cancers. Two alternatively spliced transcript variants encoding different isoforms have been observed.

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DDX42 is a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX42 is a ATP-dependent RNA helicase. DDX42 binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. It also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein.This gene encodes a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. Two transcript variants encoding the same protein have been identified for this gene.

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PPIA is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is a cyclosporin binding-protein. It may play a role in cyclosporin A-mediated immunosuppression. This protein can interact with several HIV proteins including p55 gag, Vpr, and capsid protein. It has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported. Three alternatively spliced transcript variants encoding two distinct isoforms have been observed.

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LMAN1 is a type I integral membrane protein localized in the intermediate region between the endoplasmic reticulum and the Golgi, presumably recycling between the two compartments. The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of animal cells. Mutations in its gene are associated with a coagulation defect. Using positional cloning, its gene was identified as the disease gene leading to combined factor V-factor VIII deficiency, a rare, autosomal recessive disorder in which both coagulation factors V and VIII are diminished.The protein encoded by this gene is a type I integral membrane protein localized in the intermediate region between the endoplasmic reticulum and the Golgi, presumably recycling between the two compartments. The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of animal cells. Mutations in the gene are associated with a coagulation defect. Using positional cloning, the gene was identified as the disease gene leading to combined factor V-factor VIII deficiency, a rare, autosomal recessive disorder in which both coagulation factors V and VIII are diminished.

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Eukaryotic translation initiation factor 2 (EIF-2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. EIF-2 is composed of three subunits, alpha, beta, and gamma, with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the EIF-2 complex for another round of initiation.Western blots using two different antibodies against two unique regions of this protein target confirm the same apparent molecular weight in our tests.Eukaryotic translation initiation factor 2 (EIF-2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. EIF-2 is composed of three subunits, alpha, beta, and gamma, with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the EIF-2 complex for another round of initiation. 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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FBL is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing preribosomal RNA. It is associated with the U3, U8, and U13 small nuclear RNAs and is located in the dense fibrillar component (DFC) of the nucleolus. FBL contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing preribosomal RNA. It is associated with the U3, U8, and U13 small nuclear RNAs and is located in the dense fibrillar component (DFC) of the nucleolus. The encoded protein contains an N-terminal repetitive domain that is rich in glycine and arginine residues, like fibrillarins in other species. Its central region resembles an RNA-binding domain and contains an RNP consensus sequence. Antisera from approximately 8% of humans with the autoimmune disease scleroderma recognize fibrillarin.

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Recognizes proteins of 33, 35 and 41kDa, which are identified as various isoforms of CD74/CLIP. Its epitope is localized in the extracellular domain of CD74. CD74/CLIP is a type II transmembrane protein which binds to the peptide binding groove of newly synthesized MHC class II alpha/beta heterodimers and prevents their premature association with endogenous polypeptides. The molecule plays a critical role in the presentation of peptides, by the MHC class II antigens, to CD4 positive lymphocytes. CD74/CLIP is expressed on MHC class II positive cells including B cells, a subset of activated T cells, monocytes, and dendritic cells and by various types of carcinomas. It is expressed primarily by antigen presenting cells, such as B-lymphocytes (from before the pre-B cell stage to before the plasma cell stage), macrophages, and monocytes, and many epithelial cells. Anti-CD74/CLIP stains predominantly germinal center lymphocytes and B-cell lymphomas, but rarely T-cell lymphomas and has been shown to be useful in differentiating atypical fibroxanthoma (-) from malignant fibrous histiocytoma (+).

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PITX3 is a member of the RIEG/PITX homeobox family, which is in the bicoid class of homeodomain proteins. Members of this family act as transcription factors. Mutations of PITX3 have been associated with anterior segment mesenchymal dysgenesis (ASMD) and congenital cataracts. PITX3 is involved in lens formation during eye development.This gene encodes a member of the RIEG/PITX homeobox family, which is in the bicoid class of homeodomain proteins. Members of this family act as transcription factors. Mutations of this gene have been associated with anterior segment mesenchymal dysgenesis (ASMD) and congenital cataracts. This protein is involved in lens formation during eye development. This gene encodes a member of the RIEG/PITX homeobox family, which is in the bicoid class of homeodomain proteins. Members of this family act as transcription factors. This protein is involved in lens formation during eye development. Mutations of this gene have been associated with anterior segment mesenchymal dysgenesis and congenital cataracts. 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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Oncostatin M is a member of the IL6 family of cytokines. Functional receptors for IL6 family cytokines are multisubunit complexes involving members of the hematopoietin receptor superfamily. Many IL6 cytokines utilize gp130 as a common receptor subunit. OSM binds to the gp130 receptor subunit and, in association with the leukemia inhibitory factor receptor, induces a proliferative response in permissive cells. OSMR is an alternative subunit (for an OSM receptor complex (a heterodimer of gp130 and OSMR) that is activated by OSM but not by LIF. Oncostatin M is a member of the IL6 family of cytokines. Functional receptors for IL6 family cytokines are multisubunit complexes involving members of the hematopoietin receptor superfamily. Many IL6 cytokines utilize gp130 as a common receptor subunit. OSM binds to the gp130 receptor subunit and, in association with the leukemia inhibitory factor receptor, induces a proliferative response in permissive cells. OSMR is an alternative subunit (for an OSM receptor complex (a heterodimer of gp130 and OSMR) that is activated by OSM but not by LIF. 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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Neuregulin 1 (NRG1) interacts with the NEU/ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues.Neuregulin 1 (NRG1) was originally identified as a 44-kD glycoprotein that interacts with the NEU/ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. It is known that an extraordinary variety of different isoforms are produced from the NRG1 gene by alternative splicing. These isoforms include heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). They are tissue-specifically expressed and differ significantly in their structure. The HRG isoforms all contain immunoglobulin (Ig) and epidermal growth factor-like (EGF-like) domains. GGF and GGF2 isoforms contain a kringle-like sequence plus Ig and EGF-like domains; and the SMDF isoform shares only the EGF-like domain with other isoforms. The receptors for all NRG1 isoforms are the ERBB family of tyrosine kinase transmembrane receptors. Through interaction with ERBB receptors, NRG1 isoforms induce the growth and differentialtion of epithelial, neuronal, glial, and other types of cells.

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BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.

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GPHN is a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described; however, the full-length nature of all transcript variants is not currently known. This gene encodes a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the encoded protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described; however, the full-length nature of all transcript variants is not currently known.

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CCT5 is a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. 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 nuclear orphan receptors NR2C1 represses transcription and binds DNA as a homodimer. NR2C1 binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. NR2C1 may function as a negative modulator to suppress androgen receptor function in prostate cancer. NR2C1 may exert an important repressor in regulating ER activity in mammary glands. The nuclear orphan receptors TR2 (NR2C1) and TR4 form a heterodimer that binds to the epsilon and gamma globin promoter DR1 sites This gene encodes a nuclear hormone receptor characterized by a highly conserved DNA binding domain (DBD), a variable hinge region, and a carboxy-terminal ligand binding domain (LBD) that is typical for all members of the steroid/thyroid hormone receptor superfamily. This protein also belongs to a large family of ligand-inducible transcription factors that regulate gene expression by binding to specific DNA sequences within promoters of target genes. Multiple alternatively spliced transcript variants have been described, but the full-length nature of some of these variants has not been determined.

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NR0B1 is a protein that contains a DNA-binding domain. The protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in its gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism.This gene encodes a protein that contains a DNA-binding domain. The encoded protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in this gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism.This gene encodes a protein that contains a DNA-binding domain. The encoded protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in this gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism. 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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PCBP4 is a member of the KH-domain protein subfamily. Proteins of this subfamily, also referred to as alpha-CPs, bind to RNA with a specificity for C-rich pyrimidine regions. Alpha-CPs play important roles in post-transcriptional activities and have different cellular distributions. This gene is induced by the p53 tumor suppressor, and the protein can suppress cell proliferation by inducing apoptosis and cell cycle arrest in G (2)-M.This gene encodes a member of the KH-domain protein subfamily. Proteins of this subfamily, also referred to as alpha-CPs, bind to RNA with a specificity for C-rich pyrimidine regions. Alpha-CPs play important roles in post-transcriptional activities and have different cellular distributions. This gene is induced by the p53 tumor suppressor, and the encoded protein can suppress cell proliferation by inducing apoptosis and cell cycle arrest in G (2)-M. This gene's protein is found in the cytoplasm, yet it lacks the nuclear localization signals found in other subfamily members. Multiple alternatively spliced transcript variants have been described, but the full-length nature for only some has been determined.

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The protein encoded by CDC2 is a member of the Ser/Thr protein kinase family. This protein is a catalytic subunit of the highly conserved protein kinase complex known as M-phase promoting factor (MPF), which is essential for G1/S and G2/M phase transitions of eukaryotic cell cycle. Mitotic cyclins stably associate with this protein and function as regulatory subunits. The kinase activity of this protein is controlled by cyclin accumulation and destruction through the cell cycle. The phosphorylation and dephosphorylation of this protein also play important regulatory roles in cell cycle control. The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein is a catalytic subunit of the highly conserved protein kinase complex known as M-phase promoting factor (MPF), which is essential for G1/S and G2/M phase transitions of eukaryotic cell cycle. Mitotic cyclins stably associate with this protein and function as regulatory subunits. The kinase activity of this protein is controlled by cyclin accumulation and destruction through the cell cycle. The phosphorylation and dephosphorylation of this protein also play important regulatory roles in cell cycle control.

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LGTN is a protein receptor that localizes phosphoglycoproteins within endosomes and at the cell periphery. This trafficking receptor for phosphoglycoproteins may play a role in neuroplasticity by modulating cell-cell interactions, intracellular adhesion, and protein binding at membrane surfaces. In hippocampal neurons, long-lasting down-regulation of ligatin mRNA levels occurs via post-transcriptional RNA processing following glutamate receptor activation. This protein contains single PUA and SUI1 domains and these domains may function in RNA binding and translation initiation, respectively.This gene encodes a protein receptor that localizes phosphoglycoproteins within endosomes and at the cell periphery. This trafficking receptor for phosphoglycoproteins may play a role in neuroplasticity by modulating cell-cell interactions, intracellular adhesion, and protein binding at membrane surfaces. In hippocampal neurons, long-lasting down-regulation of ligatin mRNA levels occurs via post-transcriptional RNA processing following glutamate receptor activation. This protein contains single PUA and SUI1 domains and these domains may function in RNA binding and translation initiation, respectively.