127964 Results for: "Bioss"

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Anti-ATG7 Rabbit Polyclonal Antibody

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Anti-CYP7A1 Rabbit Polyclonal Antibody

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Anti-MMP8 Rabbit Polyclonal Antibody

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Anti-KDM5B Rabbit Polyclonal Antibody

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Anti-KCNH1 Rabbit Polyclonal Antibody

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Anti-IL17RB Rabbit Polyclonal Antibody

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Anti-CSN2 Rabbit Polyclonal Antibody

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Twinkle, also known as PEO1 (Progressive external ophthalmoplegia 1 protein), PEOA3, SANDO or TWINL, is a mitochondrial protein that functions as a 5’-3’ nucleotide-dependent DNA helicase. Colocalized with mtDNA (mitochondrial DNA) in mitochondrial nucleoids, Twinkle is important in the metabolism and maintenance of mtDNA, playing a crucial role in the regulation of mtDNA copy numbers. Twinkle is expressed at high levels in testis, pancreas and skeletal muscle and exists as three isoforms due to alternative splicing events. Defects in the gene encoding Twinkle are the cause of two conditions: progressive external ophthalmoplegia with mitochondrial DNA deletions autosomal dominant 3 (PEOA3) and sensory ataxic neuropathy dysarthria and ophthalmoparesis (SANDO). PEOA3 is characterized by ptosis and weak muscles, while SANDO is characterized by ophthalmoparesis, dysarthria and sensory ataxic neuropathies.

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Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.

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Anti-BEST4 Rabbit Polyclonal Antibody

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Receptor for ASNA1/TRC40-mediated insertion of tail-anchored (TA) proteins into the ER membrane.

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Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.

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Mapping to chromosome 21, the FASP1 gene (FAPP1-associated protein 1) encodes a 233 amino acid protein that is homologous to the fission yeast protein Mis18. In yeast, Mis18 is localized to the centrosome and forms a complex with Mis16 to maintain the deacetylated state of histones specifically in the central core of centromeres. FASP1, also known as Protein Mis18-alpha and C21orf45, is required for the recruitment of CENP-A to centrosomes and is thereby essential for normal chromosome segregation during mitosis. With expression in testis, FASP1 exists as a homodimer, a heterodimer with MIS18B or is present in a complex containing other Mis18 family members. FASP1 has been shown to bind to pp5644 in Hela cells, where overexpression of pp5644 leads to inhibited growth and colony formation.

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The human augmin complex (HAUS) is an evolutionarily conserved 8-subunit protein complex that was initially discovered in Drosophila. The HAUS complex is essential for microtubule generation, centrosome integrity, mitotic spindle assembly and completion of cytokinesis. HAUS6 (HAUS augmin-like complex, subunit 6), also known as FAM29A or Dgt6, is a 955 amino acid component of the augmin complex. Required for mitotic progression, HAUS6 localizes to cytoplasm, cytoskeleton, mitotic spindle microtubules and interphase centrosomes, and undergoes post-translational phosphorylation following mitosis on multiple serine and threonine residues. HAUS6 exists as two alternatively spliced isoforms that are encoded by a gene located on human chromosome 9.

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The protein encoded by this gene is part of a complex of proteins that constitute adherens junctions (AJs). AJs are necessary for the creation and maintenance of epithelial cell layers by regulating cell growth and adhesion between cells. The encoded protein also anchors the actin cytoskeleton and may be responsible for transmitting the contact inhibition signal that causes cells to stop dividing once the epithelial sheet is complete. Finally, this protein binds to the product of the APC gene, which is mutated in adenomatous polyposis of the colon. Mutations in this gene are a cause of colorectal cancer (CRC), pilomatrixoma (PTR), medulloblastoma (MDB), and ovarian cancer. Three transcript variants encoding the same protein have been found for this gene.[provided by RefSeq, Oct 2009].

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MPG (N-methylpurine DNA glycosylase, or 3-methyladenine (3MeA) DNA glycosylase) repairs the 3MeA lethal lesion blocking DNA replication in Escherichia coli. Analysis of human cDNA libraries found a cDNA that would hybridize to human genomic DNA but not to E. coli or yeast DNA. This MPG gene has been mapped to human chromosome 16 by analysis of a panel of DNAs from mouse/human and hamster/human hybrid cell lines.

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SYF2 is a nuclear protein that interacts with cyclin D-type binding-protein 1, which is thought to be a cell cycle regulator at the G1/S transition. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

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Fused toes protein homolog (FTS), also known as AKT-interacting protein (AKTIP) and Ft1, is a 292 amino acid protein that localizes to the cytoplasm and the cell membrane. A member of the ubiquitin-conjugating enzyme family, FTS binds directly to AKT1 to regulate apoptosis in a cell population. AKT1 is a protein that plays a critical role in a number of cellular responses, such as cell growth, protein synthesis, and antiapoptotic signaling. The interaction of FTS and AKT1 enhances the phosphorylation and activation of AKT1, which, through an AKT1/GSK-3∫/NFATc1 signaling cascade, results in the increased production of the proapoptotic hormone Fas ligand and thus an increase in apoptosis.

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The Gab family of adaptor proteins function as molecular scaffolds that mediate protein recrutiment to RTKs (1–3). Cytokine/growth factor triggering of protein tyrosine kinase receptors (RTKs) initiates signaling cascades that progress to the nucleus where signals for activation, proliferation and differentiation occur (1–3). This scaffolding mechanism represents a critical link in cytokine/growth factor signaling routes. Gab1-3 contain pleckstrin homology and potential binding sites for SH2 and SH3 domain-containing proteins (1,4,5). The recruitment of signaling partners to Gab family members is phosphorylation dependent (1,4). Insulin receptor and EGF-receptor signaling are among the cascades that rely on Gab family members to elicit a nuclear response to an extracellular stimulus (6,7). The human Gab3 gene maps to chromosome Xq28 and encodes a 586 amino acid protein (5).

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FTSJ1 is a 329 amino acid nucleolar protein belonging to the RlmE family and methyltransferase superfamily. Expressed in adult thalamus, hippocampus, amygdala, corpus callosum and caudate nucleus, as well as fetal kidney, lung, liver, brain and lung, FTSJ1 plays a role in rRNA modification and processing. FTSJ1 exists as multiple spliced isoforms which are encoded by a gene located on human chromosome Xp11.23. Notably, defects in the gene encoding FTSJ1 are the cause of mental retardation X-linked type 44 (MRX44) and nonsyndromic X-linked mental retardation (MRX9).

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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 FBP1 (FUSE-binding protein or far upstream element-binding protein) to FUSE is necessary for c-Myc expression, indicating that FBP1 functions as a growth-dependent regulator of c-Myc expression. Isolated from proliferating HL-60 cells, FBP1 (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 FBP1 is detected in undifferentiated cells and is substantially decreased following cellular differentiation.

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Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

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Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.

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This gene encodes a CXC chemokine receptor specific for stromal cell-derived factor-1. The protein has 7 transmembrane regions and is located on the cell surface. It acts with the CD4 protein to support HIV entry into cells and is also highly expressed in breast cancer cells. Mutations in this gene have been associated with WHIM (warts, hypogammaglobulinemia, infections, and myelokathexis) syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. Monomer. Can form dimers.

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Anti-LZTFL1 Rabbit Polyclonal Antibody

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Anti-TNFRSF10D Rabbit Polyclonal Antibody

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Anti-INSR Rabbit Polyclonal Antibody

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Anti-MYLK Rabbit Polyclonal Antibody

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Anti-CDC7 Rabbit Polyclonal Antibody

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Anti-HCLS1 Rabbit Polyclonal Antibody