127964 Results for: "Bioss"

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Protein-kinase-C-related kinases (PRKs) are part of the lipid-regulated protein kinases (PKC) which also include liver PAK & PKN. Human PRK1 and PRK2 share structurally similar catalytic domains, but less similar N-terminal regulatory regions suggesting different regulatory domain functions. PRK1 and PRK2, as well as a third member of this family, PRK3, show distinct patterns of expression in adult tissues. Additionally, the serine-threonine kinase PRK2 can be specifically cleaved by caspase-3 (and/or caspase-3-like subfamily members) during apoptosis

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The inositol polyphosphate 5-phosphatases selectively remove the phosphate from the 5-position of various phosphatidylinositols, which generate second messengers in response to extracellular signals. Synaptojanins are characterized by an N-terminal SAC1-like sequence, a central 5-phosphate domain, and a unique C-terminal sequence and have been shown to use phosphatidylinositol 4,5-bisphosphate as a substrate. Synaptojanins exist as two isoforms, synaptojanin 1 and 2, which differ in the C-terminal domain, and each isoform has multiple variants produced by alternative splicing. Synaptojanin 1 is expressed as two major forms: the shorter is found in brain while the longer is expressed in peripheral tissues. Eight splice variants of synaptojanin 2 have been detected, including a brain specific isoform. Synaptojanins are thought to participate in the endocytosis of synaptic vesicles and the regulation of the actin cytoskeleton.

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Syntaxin 13 is an integral membrane protein that belongs to the t-SNARE family, a group of proteins involved in protein transport. Confocal immunofluoresence and electron microscopy studies have shown that syntaxin 13 is primarily localized to tubular early and recycling endosomes, where it colocalizes with transferrin receptor, and it is also localized in endosomal vacuoles. Syntaxin 13 has been found to be expressed in all tissues, with higher levels of the protein found in brain, lung, spleen, thymus and testes. Immunoprecipitation studies show that syntaxin 13 complexes with beta-SNAP, VAMP2/3, and SNAP25. The binding of this complex to alpha-SNAP and NSF is terminated in the presence of ATP. These results suggest that syntaxin 13 is a SNARE protein which mediates the recycling protein flow through tubulo vesicular recycling endosomes.

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May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.

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Anti-MAPKAPK2 Rabbit Polyclonal Antibody

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Anti-CTF1 Rabbit Polyclonal Antibody

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Anti-FUS Rabbit Polyclonal Antibody

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Anti-IL17B Rabbit Polyclonal Antibody

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TNFRSF14 is a type I membrane protein belonging to the TNF receptor superfamily. This receptor mediates herpes virus entry into cells during infection. TNFRSF14 is able to inhibit the proliferation, activation, and cytokine production of T cells. It has an extracellular domain containing several cysteine-rich repeats and a short cytoplasmic region containing a TRAF (TNF receptor-associated factor) interaction domain. The extracellular domain of TNFRSF14 interacts with the herpes simplex virus envelope glycoprotein D. TNFRSF14 binds two cellular ligands: lymphotoxin alpha and LIGHT. LIGHT is a transmembrane protein expressed and shed from the surface of activated T cells, exhibits inducible expression, and competes with HSV glycoprotein D for HVEM, a receptor expressed by T lymphocytes. The LIGHT:TNFRSF14 interaction controls immune response functions by cell death induction as well as cell activation. TNFRSF14 is expressed by peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells.

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Anti-C9orf116 Rabbit Polyclonal Antibody

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Anti-RAP2B Rabbit Polyclonal Antibody

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C8orf77 (chromosome 8 open reading frame 77) is a 211 amino acid protein encoded by a gene that maps to human chromosome 8q24.3. Consisting of nearly 146 million bases, chromosome 8 encodes about 800 genes. Translocation of portions of chromosome 8 with amplifications of the c-Myc gene are found in some leukemias and lymphomas, and are typically associated with a poor prognosis. Portions of chromosome 8 have been linked to schizophrenia and bipolar disorder. Trisomy 8, also known as Warkany syndrome 2, most often results in early miscarriage but is occasionally seen in a mosaic form in surviving patients who suffer to a varying degree from a number of symptoms including retarded mental and motor development, and certain facial and developmental defects. WRN is a DNA helicase encoded by chromosome 8 and shown defective in those with the early aging disorder Werner syndrome. Chromosome 8 is also associated with Pfeiffer syndrome, congenital hypothyroidism and Waardenburg syndrome.

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GCKR is a subfamily member of the SIS (Sugar ISomerase) family of proteins. It is a regulatory protein that inhibits glucokinase in liver and pancreatic islet cells by binding non-covalently to form an inactive complex with the enzyme. This gene is considered a susceptibility gene candidate for a form of maturity-onset diabetes of the young.

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Monokine with inflammatory, pyrogenic and chemokinetic properties. Has a potent chemotactic activity for eosinophils. Binding to a high-affinity receptor activates calcium release in neutrophils.

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B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response.

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Anti-HBV D pre-S1/S2 Protein Rabbit Polyclonal Antibody

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The Src homology 3 (SH3) region is a small protein domain of approximately 60 amino acids present in a large group of proteins. In general, it exists in association with catalytic domains, as in the nonreceptor protein-tyrosine kinases and phospholipase C-? within structural proteins, such as spectrin or Myosin; and in small adapter proteins, such as Crk and GRB2. SH3 domains are often accompanied by SH2 domains of 100 amino acids, which bind to tyrosine-phosphorylated regions of target proteins, frequently linking activated growth factors to putative signal transduction proteins. The functions of SH3 domains are not as well defined. Deletion or mutation of SH3 domains generally activate the transforming potential of nonreceptor tyrosine kinases, suggesting that SH3 mediates negative regulation of an intrinsic transforming activity. 3BP1 has been identified as a protein with a high affinity proline-rich binding site for the SH3 domain of c-Abl p120. A similar putative adapter protein, designated Slap, for Src-like adapter protein, has been cloned. Slap contains a single SH2 and SH3 domain that exhibits homology with those from members of the Src kinase family. The N- and C-termini, however, are unique.

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This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized. [provided by RefSeq, Jul 2008].

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This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008].

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Ephrin B proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development. Ephrin B molecules expressed at the membrane surface bind to the Ephrin B family receptors on target cells during cell to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing Ephrin B on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of Ephrin B is thought to be a critical component of this reverse signaling event. Recent work demonstrated that Tyr331 of Ephrin B was phosphorylated in HEK293 cells after stimulation by the soluble Ephrin B2 receptor tyrosine kinase.

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eNOS is a calcium/calmodulin dependent enzyme which undergoes several post translational modifications, including acylation with myristate and palmitate, and phosphorylation on numerous residues. As with the other members of the NOS family, eNOS derives the diffusible multifunctional second messenger NO from L arginine through a series of reactions in which L citrulline is an intermediate. eNOS plays an important role in controlling vascular tone, platelet aggregation, and cardiac myocyte function.

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ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. ErbB3 is a membrane-bound protein which has a neuregulin binding domain but not an active kinase domain. It can therefore bind this ligand but cannot convey a signal into the cell via protein phosphorylation. However it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers including prostate, bladder and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. Isoform 2 lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported but they have not been thoroughly characterized. Defects in ERBB3 are the cause of lethal congenital contracture syndrome type 2 (LCCS2); also called Israeli Bedouin multiple contracture syndrome type A. LCCS2 is an autosomal recessive neurogenic form of a neonatally lethal arthrogryposis that is associated with atrophy of the anterior horn of the spinal cord.

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The erythropoietin receptor (EPOR) is a member of the cytokine receptor family. There are several isoforms including: EPOR-F (full length), EPOR-S (soluble form), and EPOR-T (truncated form). Upon erythropoietin (EPO) binding, the EPOR activates Jak2 tyrosine kinase which activates different intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. The stimulated EPOR appears to have a role in erythroid cell survival. Defects in the EPOR may produce erythroleukemia and familial erythrocytosis. A functional EPOR is found in the cardiovascular system, including endothelial cells and cardiomyocytes, and data suggest that the EPO/EPO receptor system plays an important role in cardiac function. In animal studies, treatment with EPO during ischemia/reperfusion in the heart has been shown to limit the infarct size and the extent of apoptosis.

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Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.

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HP1 alpha is a component of heterochromatin. It recognizes and binds histone H3 tails methylated at Lys-9, leading to epigenetic repression. HP1 alpha may interact with lamin B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. HP1 proteins are relatively small proteins (~25 kDa) with a conserved amino-terminal chromo domain and a structurally related carboxy-terminal motif, the chromo shadow domain. Both domains of HP1 are required for binding to native chromatin in vivo, but they contribute differentially to binding in euchromatin and heterochromatin.

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TMEM16C is a 981 amino acid multi-pass membrane protein that is encoded by a gene which maps to chromosome 11. With approximately 135 million base pairs and 1,400 genes, chromosome 11 makes up around 4% of human genomic DNA and is considered a gene and disease association dense chromosome. The chromosome 11 encoded Atm gene is important for regulation of cell cycle arrest and apoptosis following double strand DNA breaks. Atm mutation leads to the disorder known as ataxia-telangiectasia. The blood disorders Sickle cell anemia and thalassemia are caused by HBB gene mutations, while Wilms' tumors, WAGR syndrome and Denys-Drash syndrome are associated with mutations of the WT1 gene. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are also associated with defects in chromosome 11.

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This gene encodes a subunit of the anaphase-promoting complex. This complex is an E3 ubiquitin ligase that regulates progression through the metaphase to anaphase portion of the cell cycle by ubiquitinating proteins which targets them for degradation. [provided by RefSeq, Dec 2011].

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The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. ANKK1 (ankyrin repeat and kinase domain containing 1), also known as PKK2 or SGK288, is a 765 amino acid protein that belongs to the Ser/Thr protein kinase family and contains 12 ANK repeats and one protein kinase domain. Highly expressed in brain tissue and present in lower amounts in placenta and spinal cord, ANKK1 functions to catalyze the ATP-dependent phosphorylation of target proteins and is thought to play a role in alcohol and nicotine dependence. The gene encoding ANKK1 maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome.

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Members of the glutathione S-transferase (GST) family of proteins function in the detoxification of xenobiotics to protect cells against toxicant-induced damage. There are eight families of GST proteins, namely alpha, zeta, theta, kappa, mu, pi, sigma and omega, each of which are composed of proteins that have a variety of functions throughout the cell. GSTK1 (glutathione S-transferase kappa 1), also known as glutathione S-transferase subunit 13 (GST 13-13) or GSTK1-1, is a 226 amino acid ubiquitously expressed protein belonging to the kappa class of the GST superfamily that functions in cellular detoxification. Localizing to peroxisome, GSTK1 exists as a homodimer that catalyzes the conjugation of glutathione to a number of hydrophobic substrates leading to their removal from the cell.

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Anti-GLYCTK Rabbit Polyclonal Antibody