127976 Resultaten voor: "Bioss"

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Anti-CDC25C Rabbit Polyclonal Antibody

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Anti-PCGF2 Rabbit Polyclonal Antibody

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This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column (By similarity).

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The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase.

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This gene encodes a nuclear protein with a JmjC domain. JmjC domain-containing proteins are predicted to function as protein hydroxylases or histone demethylases. This protein was first identified as a putative phosphatidylserine receptor involved in phagocytosis of apoptotic cells; however, subsequent studies have indicated that it does not directly function in the clearance of apoptotic cells, and questioned whether it is a true phosphatidylserine receptor. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

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Progression of cells from interphase to mitosis involves alterations in cell structures and activities. The transition from G2 to M phase is induced by M phase promoting factor, or MPF. In M phase, many proteins are phosphorylated directly by MPF or indirectly by kinases activated by MPF. These M phase phosphoproteins (MPPs, or MPHOSPHs) permit disassembly of interphase structures and generation of M phase enzymatic activities and structures. VAM1 or MPP6 is thought to be a nucleolus specific exosome co factor, required for its role in the maturation of 5.8S rRNA.

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The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

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CDKN3 is a second dual specificity phosphatase that interacts with cyclin dependent kinases.The ability of CDKN3 to bind multiple cyclin-dependent kinases suggests that it may be a critical control element in cell cycle regulation, presumably by regulating the phosphorylation state of a Cdk or Cdk-associated protein.

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CKS1 protein binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. The CKS1 mRNA is found to be expressed in different patterns through the cell cycle in HeLa cells, which reflects a specialized role for the encoded protein. At least two transcript variants have been identified for this gene, and it appears that only one of them encodes a protein.

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SP17 is a protein present at the cell surface. The N-terminus has sequence similarity to human cAMP-dependent protein kinase A (PKA) type II alpha regulatory subunit (RIIa) while the C-terminus has an IQ calmodulin-binding motif. The central portion of the protein has carbohydrate binding motifs and likely functions in cell-cell adhesion. The protein was initially characterized by its involvement in the binding of sperm to the zona pellucida of the oocyte. Recent studies indicate that it is also involved in additional cell-cell adhesion functions such as immune cell migration and metastasis. A retrotransposed pseudogene is present on chromosome 10q22.[provided by RefSeq, Jan 2009].

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Plexin A2 is a coreceptor for SEMA3A and is necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. This coreceptor plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin in which the plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm.

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The ABL1 protooncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response. Activity of c-Abl protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR (MIM:151410) and ABL1 genes present in many cases of chronic myelogeneous leukemia. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for ABL1. The ABL1 gene is expressed as either a 6- or 7-kb mRNA transcript, with alternatively spliced first exons spliced to the common exons 2-11. [provided by RefSeq].

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CAPS2 is a 557 amino acid calcium-binding protein that is abundantly expressed, with highest expression found in placenta, testis, colon, lung and brain. CAPS2 contains three EF-hand domains and exists as three alternatively spliced isoforms. Suggested to play a role in large dense-core vesicle (LDCV) exocytosis, CAPS2 is encoded by a gene that maps to human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and trisomy 12p, which causes facial developmental defects and seizure disorders.

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The galanin family of proteins are key members for inflammatory processes and cell proliferation, and may function as potential biomarkers for colon cancer. Produced in both neuronal and nonneuronal cells in the skin, members of the galanin family include galanin, galanin-message associated peptide, galanin-like peptide and alarin. GALP, also known as galanin-like peptide, is a 116 amino acid secreted protein belonging to the galanin family. Mainly produced in the arcuate nucleus of the hypothalamus (ARC) and the posterior pituitary, GALP is thought to function in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion. GALP binds to the G-protein coupled galanin receptors, including GALR1, GALR2 and GALR3, and may also play a role in energy metabolism, with significant implications towards obesity. GALP exits as two alternatively spliced isoforms.

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PTOV1 belongs to the Mediator complex subunit 25 family, PTOV1 subfamily. It may activate transcription and is required for nuclear translocation of FLOT1. PTOV1 promotes cell proliferation. There are three named isoforms.

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Odorant receptor (Potential). May be involved in taste perception.

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Mutations in the mouse Tub gene gradually lead to obesity, strongly resembling the late-onset obesity observed in the human population. In addition to excessive deposition of adipose tissue, mice with the Tub phenotype also suffer retinal degeneration and neurosensory hearing loss. A human homolog of the Tub gene has been identified, as have three related proteins, called Tubby-like protein 1 (TULP1), TULP2 and TULP3. When compared to TULP1 and TULP2, TULP3 has a wider tissue expression and is phylogenetically more similar to Tub than either TULP1 or TULP2. TULP1, expressed specifically in the retina, maps to the chromosomal region known to be involved in retinitis pigmentosa, while TULP2 maps within the minimal interval for the rod-cone dystrophy. TULP3 maps to human chromosome 12p13, and shares 69% homology to mouse TULP3. Human RNA from testis, ovary, thyroid and spinal cord contain highly detectable levels of TULP3 transcripts. In the retina, TULP3 is expressed specifically in the inner nuclear layer and ganglion cell layer. TULP1, TULP2 and TULP3 may comprise a unique family of bipartite transcription factors.

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Anti-OR5T1 Rabbit Polyclonal Antibody

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Phocein is a 225 amino acid protein encoded by the human gene MOBKL3. Phocein belongs to the MOB1/phocein family and is phosphorylated on serine residues. Phocein is a widely expressed, highly conserved intracellular protein. The sequence of Phocein has limited homology to the sigma subunits from Clathrin adaptor complexes and contains an additional stretch bearing a putative SH3-binding domain. Phocein is usually associated with membranes but can be present in the cytosol, where it behaves as a protein complex. Phocein is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking. Due to its association with Dynamin via direct interactions with nucleotide diphosphate kinase (NDPK) and Eps15, Phocein has been implicated in vesicular trafficking, acting in particular in the endocytic process.

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The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. LRRC54 (leucine-rich repeat-containing protein 54), also known as tsukushin, TSKU or E2-induced gene 4 protein (E2IG4), is a 353 amino acid secreted protein that likely localizes to the cell membrane and extracellular compartments. Involved in extracellular secretion and intracellular transport, LRRC54 can be induced by 17-beta-estradiol. Containing nine LRR repeat and a cleavable signal peptide, the gene encoding LRRC54 maps to human chromosome 11, which houses over 1,400 genes and comprises nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that maps to chromosome 11.

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MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

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G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or may be involved in synaptogenesis or synaptic stabilization.

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KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

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May be involved in transcriptional regulation.

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The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. The ligand for the receptor is angiopoietin-1. Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis.TEK is closely related to the TIE receptor tyrosine kinase.

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Sorting nexin 1 (SNX1) is a member of a large family of hydrophilic proteins that interact with a variety of receptor types and are involved in intracellular trafficking. SNX1 and the related splice variant, SNX1A, bind the epidermal growth factor (EGF) receptor and facilitate its transport to lysosome, thereby contributing to the degradation of the receptor. SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain. These proteins are all partially associated with cellular membranes and they likewise associate with EGF, PDGF and insulin receptor tyrosine kinases. These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multi-subunit complexes. The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors.

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Fukutin, a secreted protein, is expressed in various tissues in normal individuals. Fukutin colocalizes with a Golgi marker and a granular cytoplasmic distribution, suggesting that fukutin passes through the Golgi before being packaged into secretory vesicles. Fukutin may be located in the extracellular matrix, where it interacts with and reinforces a large complex encompassing the outside and inside of muscle membranes; alternatively, as a secreted protein, fukutin may cause muscular dystrophy by an unknown mechanism. The fukutin gene is expressed at similar levels in control fetal and adult brain, but is much reduced in Fukuyama congenital muscular dystrophy (FCMD) brains. Fukutin deficiency affects the modification of glycosylation of DAG1 (α-dystroglycan), which then cannot localize or function properly and may be degraded or eluted from the extracellular surface membrane of the muscle fiber. FCMD is the first human disease known to be caused by an ancient retrotransposal integration. The gene which encodes fukutin maps to human chromosome 9q31.

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FSD1L is a 530 amino acid protein containing one B30.2/SPRY domain, one COS domain, and a fibronectin type-III domain. Existing as three alternatively spliced isoforms, FSD1L is expressed primarily in brain, with lower levels of expression found in thymus, pituitary and testis. FSD1L may function in microtubule binding during interphase and is encoded by a gene that maps to human chromosome 9q31.2. Chromosome 9 consists of about 145 million bases andd comprises approximately 4% of the human genome and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype.

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Activation of FUSE, the far-upstream element, is required for the proper ex-pression of the mammalian gene c-Myc in undifferentiated cells. The binding of FBP (FUSE-binding protein or Far upstream element binding protein) to FUSE is necessary for c-Myc expression, indicating that FBP functions as a growth-dependent regulator of c-Myc expression. Isolated from proliferating HL60 cells, FBP, FBP2, and FBP3 comprise a family of single-stranded DNA-binding proteins that specifically bind to FUSE elements. The FBP transcription factors share a conserved central DNA-binding domain and show significant homology in their carboxyl-terminal activation domains. Expression of FBP is detected in undifferentiated cells and is substantially decreased following cellular differentiation.

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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.