92236 Results for: "Bioss"

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ADP-ribosylation factors (ARFs) are highly conserved guanine nucleotide-binding proteins that enhance the ADP-ribosyltransferase activity of cholera toxin. ARF抯 are important in eukaryotic vesicular trafficking pathways and activating phospholipase D. ARL4 (ADP-ribosylation factor-like protein 4A) is a member of the ARF-like protein (ARL) subfamily of small GTPases. It contains a C terminal nuclear localization signal (NLS) region that interacts with Importin-? ARL4 localizes to the nucleus and is found in a variety of tissues, but is predominantly expressed in spermatogonia and Sertoli cells. It is most closely related to ARL6 and ARL7. Unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4 may play a role in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.

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Reversible acetylation of highly conserved lysine residues within the N-terminal tail domains of core histones, plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs). Histone deacetylases activities are often, but not always, associated with transcriptional repression and nucleosomal condensations. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1 and Rb family of transcription factors, transcriptional repressors and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by certain oncoproteins may occur in certain neoplastic diseases. Belongs to the histone deacetylase family.

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The transcriptional enhancer factor-1 (TEF-1) family of transcription factors regulate tissue-specific gene expression in muscle and placenta. The mechanism whereby TEF-1 confers tissue specificity depends largely on the interaction of TEF-1 with tissue-specific cofactors. Transcription cofactor Vgl-4 (vestigial-like protein 4) is a 290 amino acid nuclear protein that interacts with TEF-1 and MEF-2. Vgl-4 is the only member of the vestigial-like family that is expressed in heart. Overexpression of Vgl-4 in cardiac myocytes interferes with basal expression and ?-adrenergic receptor-dependent activation of a TEF-1 dependent skeletal ?actin promoter. This suggests that Vgl-4 counteracts ?-adrenergic activation of gene expression in cardiomyocytes. There are two isoforms of Vgl-4 that are produced as a result of alternative splicing events.

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The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.

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IKK beta (I-Kappa-B kinase-beta) is a member of the IKK complex which is composed of IKK alpha, IKK beta, IKK gamma and IKAP. Phosphorylation of I-Kappa-B on a serine residue by the IKK complex frees NF-kB from I-Kappa-B and marks it for degradation via ubiquination. IKK beta has been shown to activate NF-kB and phosphorylate IKB alpha and beta. Phosphorylation of 2 sites at the activation loop of IKK beta is essential for activation of IKK by TNF and IL1. Once activated, IKK beta autophosphorylates which in turn decreases IKK activity and prevents prolonged activation of the inflammatory response. Additionally, IKK beta activity can also be regulated by MEKK1.

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The serine proteinase inhibitors (serpins) compose a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. SERPINB12 appears to be an inhibitor of trypsin-like serine proteinases, including mast cell tryptases.

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As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. Uncleaved haptoglogin, also known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens.

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The helix-loop-helix (HLH) structures are known motifs commonly found in membrane-active and DNA-binding proteins. The helix-loop-helix proteins HEN1 and HEN2 are DNA-binding proteins that may be involved in cell-type determination in the early nervous system. Studies of expression in normal tissues have demonstrated expression of NHLH1/NSCL-1 and NHLH2/NSCL-2, the genes encoding HEN1 and HEN2, in the developing central and peripheral nervous system, specifically in developing neurons.

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ID (inhibitor of DNA binding) HLH proteins lack a basic DNA-binding domain but are able to form heterodimers with other HLH proteins, thereby inhibiting DNA binding. ID-3 inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. May inhibit other transcription factors.

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GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules.

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Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells.

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Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

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Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). MARCH9 (membrane-associated ring finger (C3HC4) 9), also known as RNF179, is a 346 amino acid multi-pass membrane protein that localizes to the golgi apparatus and contains one RING-CH-type zinc finger. Expressed ubiquitously, MARCH9 exists as a homodimer and functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and is thought to promote the degradation of target proteins, such as CD4 and MHC-I. Multiple isoforms of MARCH9 exist due to alternative splicing events.

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Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.

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Sox genes comprise a family of genes that are related to the mammalian sex determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. Sox genes encode putative transcriptional regulators implicated in the decision of cell fates during development and the control of diverse developmental processes. The highly complex group of Sox genes cluster at least 40 different loci that rapidly diverged in various animal lineages. At present, 30 Sox genes have been identified. Members of this family have been shown to be conserved during evolution and to play key roles during animal development. Some are involved in human diseases, including sex reversal.

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BCL2 is an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants (alpha and beta) produced by alternate splicing, differ in their C-terminal ends. BCL2 suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. It regulates cell death by controlling the mitochondrial membrane permeability. It appears to function in a feedback loop system with caspases. BCL2 inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF1). It can form homodimers, and heterodimers with BAX, BAD, BAK and BclX(L). Heterodimerization with BAX requires intact BH1 and BH2 domains, and is necessary for anti-apoptotic activity.

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C19orf45 is a 505 amino acid protein that is encoded by a gene located on human chromosome 19. Chromosome 19 consists of approximately 63 million bases and makes up over 2% of human genomic DNA. Chromosome 19 includes a diversity of interesting genes and is recognized for having the greatest gene density of the human chromosomes. It is the genetic home for a number of immunoglobulin superfamily members including the killer cell and leukocyte Ig-like receptors, a number of ICAMs, the CEACAM and PSG family, and Fcα receptors. Key genes for eye color and hair color also map to chromosome 19. Peutz-Jeghers syndrome, spinocerebellar ataxia type 6, the stroke disorder CADASIL, hypercholesterolemia and insulin-dependent diabetes have been linked to chromosome 19. Translocations with chromosome 19 and chromosome 14 can be seen in some lymphoproliferative disorders and typically involve the proto-oncogene BCL3.

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The tetratricopeptide repeat (TPR) motif is a degenerate, 34 amino acid sequence found in many proteins and acts to mediate protein-protein interactions in various pathways. At the sequence level, there can be up to 16 tandem TPR repeats, each of which has a helix-turn-helix shape that stacks on other TPR repeats to achieve ligand binding specificity. EDRF1 (erythroid differentiation-related factor 1), also known as C10orf137 (chromosome 10 open reading frame 137), is a 1,238 amino acid protein containing two TPR repeats. Localizing to nucleus, EDRF1 is involved in transcriptional activation of globin genes by regulating DNA-binding activity of GATA-1 transcription factor. EDRF1 may also play an important role in organ development and histological differentiation. EDRF1 exists as four alternatively spliced isoforms and is encoded by a gene mapping to human chromosome 10q26.13.

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The HIRA protein shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of the HIRA protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding HIRA-interacting proteins, or HIRIPs, have been identified. In vitro, the protein encoded by this gene binds HIRA, as well as H2B and H3 core histones, indicating that a complex containing HIRA-HIRIP3 could function in some aspects of chromatin and histone metabolism. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[provided by RefSeq, Aug 2011].

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CXCL16 acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidised low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. It induces a strong chemotactic response and calcium mobilisation. It binds to CXCR6/Bonzo.

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Anti-INHBB Rabbit Polyclonal Antibody

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Anti-IRF7 Rabbit Polyclonal Antibody

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Anti-SLC39A6 Rabbit Polyclonal Antibody

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Anti-Integrin Alpha 5 + Beta 3 Rabbit Polyclonal Antibody

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Anti-CUBN Rabbit Polyclonal Antibody

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Anti-RHOC Rabbit Polyclonal Antibody

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Anti-MYOD Rabbit Polyclonal Antibody

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Anti-STAT5 Rabbit Polyclonal Antibody

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Anti-ST6GAL1 Rabbit Polyclonal Antibody

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HHLA1.