127977 Ergebnisse für: "Bioss"

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The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. A wide range of enzymes facilitate in the proteolytic Ub pathway, including monoclonal nonspecific suppressor factor-beta (MNSF-beta), a subunit of MNSF, which is a lymphokine product of a murine T cell hybrid-oma that restricts the production of LPS-induced immunoglobulin secreting cells in an antigen-nonspecific manner. MNSF-beta is a ubiquitin-like fusion protein consisting of the ribosomal protein S30 and a protein that shares 36% sequence identity with ubiquitin. This ubiquitin-like segment (Ubi-L) can be cleaved from MNSF-beta in the cytosol.

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Fanconi anemia (FA) is an autosomal recessive disorder characterized by bone marrow failure, birth defects and chromosomal instability. At the cellular level, FA is characterized by spontaneous chromosomal breakage and a unique hypersensitivity to DNA cross-linking agents. At least eight complementation groups (A-G) have been identified and six FA genes (for subtypes A, C, D2, E, F and G) have been cloned. The FA proteins lack sequence homologies or motifs that could point to a molecular function. The cellular accumulation of FA proteins, including FANCA and FANCG, is subject to regulation by TNF alpha signaling. Phosphorylation of FANC (Fanconi anemia complementation group) proteins is thought to be important for the function of the FA pathway. FANCA, also known as FACA and FANCH, associates with the Brm-related gene 1 (BRG1) product, a subunit of the SWI/SNF complex which remodels chromatin structure through a DNA-dependent ATPase activity. FANCA is mainly expressed in lymphoid tissues, testis and ovary. The amino-terminal region of the FANCA protein is required for FANCG binding, FANCC binding, nuclear localization and functional activity of the complex. The human FANCA gene maps to chromosome 16q24.3 and encodes a 1,455 amino acid protein.

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Belonging to the F-box family of proteins, FBXO45 is a 286 amino acid protein that contains one C-terminal F-box domain. F-box proteins are critical components of the SCF (Skp1-CUL-1-F-box protein)-type E3 ubiquitin ligase complex and are involved in substrate recognition and protein recruitment for ubiquitination. They are members of a larger family of proteins that are involved in the regulation of a wide variety of cellular mechanisms, including the cell cycle, the immune response, signaling cascades and developmental processes. They function by targeting proteins, such as cyclins, cyclin-dependent kinase inhibitors, I˚B-å and ∫-catenin, for degradation by the proteasome after ubiquitination. Via its F-box domain, FBXO45 can directly interact with Skp1 p19 and CUL-1. FBXO45 has been shown to be an estrogen-induced gene.

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Transcription repressor. Required for the specification of corticospinal motor neurons and other subcerebral projection neurons. May play a role in layer and neuronal subtype-specific patterning of subcortical projections and axonal fasciculation. Controls the development of dendritic arborization and spines of large layer V pyramidal neurons. May be involved in innate immunity (By similarity).

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Zic5 (zinc finger protein of the cerebellum 5) is a C2H2 zinc finger transcription factor that influences development of the neural crest. Zic family members are abundant in developing and adult cerebellum. Zic family members are important during development, and have been associated with X-linked visceral heterotaxy and holoprosencephaly type 5. Zic5 is closely linked to Zic2, a related family member on chromosome 13.

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AGPAT6 is a novel glycerolipid acyltransferase of the ER, which is crucial for the production of milk fat by the mammary gland. It converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.

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The Raf family of serine/threonine specific kinases is comprised of three members (aRaf, bRaf, and cRaf) that play a critical role in regulating cell growth and differentiation, and couple growth factor receptor stimulation to nuclear transcription factors via the Ras/mitogen activated protein kinase (MAPK) pathway. cRaf kinase (also known as Raf1) is a small GTPase like kinase of 73 kDa, and is a signal transducer of multiple extracellular stimuli that is regulated by several pathways, and that once activated, phosphorylates MEK which in turn phosphorylates ERK. Raf1 is involved in the transduction of mitogenic signals from the cell membrane to the nucleus. It is part of the Ras dependent signaling pathway from receptors to the nucleus.

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Isoform 2 is expressed in colon, breast, prostate, pancreas and kidney tumor cell lines. Isoform 2 is expressed at high levels in kidney, prostate, brain, small intestine and pancreas, at moderate levels in placenta and colon, at low levels in lung, liver and heart, and at very low levels in spleen, thymus, peripheral mononuclear blood cells, testis and ovary.

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The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core 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. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase 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 non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17.

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The Makorins are a family of putative ribonucleoproteins containing two to four C3H zinc fingers that may confer RNA-binding. In addition, they contain a C3HC4 RING zinc finger that allows them to function as E3 ubiquitin ligases. Makorin-2, also known as RNF62, HSPC070 or MKRN2, is a widely expressed, evolutionarily conserved protein with four C3H-type zinc fingers (three at the N-terminus and one at the C-terminus), one RING-type zinc finger and a cysteine and histidine motif similar to that found in Makorin-1. In Xenopus, Makorin-2 functions, via PI 3-kinase/Akt signaling, as a negative regulator of neurogenesis. In humans, Makorin-2 is overexpressed in various cancer cell lines, suggesting a possible role of Makorin-2 in tumor progression. In addition, Makorin-2 is co-expressed with Raf-1 in the same tissues and cell lines.

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Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro.Tissue specificity:Highly expressed in heart and skeletal muscle.

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MST1R/Ron, a HGF Receptor/MET-type protein kinase, mediates the biological activities of macrophage-stimulating protein (MSP), a multifunctional cytokine that regulates cell adhesion, motility, growth, and survival. The protein is a membrane-spanning, disulfide-linked heterodimer, which results from cleavage of a glycosylated precursor into 35-kD (alpha) and 150-kD (beta) subunits. Ligand binding results in tyrosine phosphorylation of the beta chain. In knockout studies, MST1R/RON (-/-) mice failed to survive past the periimplantation period. The MST1R/RON gene has been mapped to 3p21, a region of frequent deletion or mutation in small cell lung and renal carcinoma, and has been implicated in the progression of several epithelial cancers. Ron expression has been documented in many normal human tissues. ESTs have been isolated from several tissue libraries, including normal colon, mouth, prostate, and testis and cancerous colon, prostate, stomach, and uterus.

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PLK5 (Serine/threonine-protein kinase PLK5) belongs to the protein kinase superfamily and Ser/Thr protein kinase family and CDC5/Polo subfamily. PLK5P contains 1 POLO box domain and 1 Serine/Threonine protein kinase catalytic domain.

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Anti-PDZD5A Rabbit Polyclonal Antibody

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Anti-ABHD15 Rabbit Polyclonal Antibody

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ADCK2 (aarF domain containing kinase 2), also known as AARF, is a 626 amino acid single-pass membrane protein belonging to the protein kinase superfamily and the ADCK protein kinase family. The ADCK family consists of five paralogs in human (ADCK1-5). Encoded by a gene that maps to human chromosome 7q34, ADCK2 contains one protein kinase domain. ADCK2 participates in ATP and nucleotide binding, transferase functions and protein serine/threonine kinase activities. Expression of ADCK2 inversely correlates with cellular viability, suggesting elevated expression of ADCK2 may be essential for tumour survival. ADCK2 is necessary for cell proliferation of glioblastoma multiforme (GBM), a fatal primary brain tumor containing countless genetic and epigenetic alterations.

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ABCA5 is a member of the superfamily of ATP binding cassette (ABC) transporters. ABC proteins transport various molecules across extra and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White). ABCA5 is a member of the ABC1 subfamily. Members of the ABC1 subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. ABCA5 is localized in the lysosome, late endosome and Golgi apparatus membrane and is thought to play a role in the processing of autolysosomes.

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Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.Involvement in disease:Defects in ALAD are the cause of acute hepatic porphyria (AHP). AHP is a form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralysis, and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.

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Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1 and CDKN1A/p21(CIP1). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis.Tissue specificity: Expressed in placenta and testis, very low expression seen in skeletal muscle. Detected in all hematopoietic tissues examined, with highest expression in thymus and bone marrow. A low level detected in the spleen and lymph node, and barely detectable level in the peripheral leukocytes. RA treatment down-regulated the expression in NT2 cell.

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The exosome is a multi-protein complex composed of several highly conserved subunits, some of which are 3’ to 5’ exoribonucleases. The complex is involved in a variety of cellular processes and is responsible for degrading unstable mRNAs that contain AU-rich elements (AREs) in their untranslated 3’ regions. DIS3, also known as RRP44, is a 958 amino acid protein that localizes to both the cytoplasm and the nucleus and contains one PINc domain. Widely expressed with highest expression in testis, DIS3 functions as a component of the exosome exoribonuclease complex and is required for processing of 7S pre-RNA into a mature nuclear complex and, ultimately, for proper mitotic progression. Abnormal expression levels of DIS3 may be associated with colon cancer, suggesting a role for DIS3 in tumorigenesis. Multiple isoforms of DIS3 exist due to alternative splicing events.

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PDZK4, also known as PDZRN4L (PDZ domain-containing RING finger protein 4-like protein) or LU1, is a 769 amino acid coiled-coil protein that contains one PDZ (DHR) domain. Encoded by a gene that maps to human chromosome Xq28, PDZK4 is conserved in dog, cow, mouse, rat and zebrafish. PDZK4 localizes to cytoplasm and is expressed specifically in adult and fetal brain. PDZK4 functions as an oncogene and is up-regulated in synovial carcinomas. Treatment of synovial sarcoma cells with small interfering RNA (siRNA) inhibits PDZK4 expression, resulting in tumor-cell growth suppression, suggesting that inappropriate expression of PDZK4 may play a role synovial sarcoma cell proliferation.The exact function of FRMPD2 is unknown. The protein contains a FERM domain: such structures are often involved in signal transduction pathways. Alternatively spliced transcript variants encoding different isoforms have been identified.

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ACBD4 is a member of the acyl-coenzyme A binding domain containing protein family. ACBD4 contains 1 ACB (acyl-CoA-binding) domain. There are three isoforms. Its function is unknown.

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SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

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Intrinsic membrane protein of small synaptic vesicles. Probable vesicular channel protein (By similarity).

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Musashi1 (Msi1) is an RNA-binding protein expressed in neural progenitor cells and neural stem cells. Msi1 is the mammalian homolog of Drosophila Musashi. The gene encoding human Msi1 encodes a 362 amino acid protein. In murine embryonic neural progenitor cells, Msi1 localizes to the cytoplasm and is downregulated during differentiation. Msi1 binds to NUMB, which encodes a membrane-associated antagonist of Notch signaling. Msi1 appears to function in the proliferation and maintenance of stem cell populations of the central nervous system. In addition to its usefulness as a marker for neural progenitor cells in normal human brains, Msi1 is also a marker for human gliomas. In rats, Msi1 is expressed in Sertoli cells of the testis and granulosa cells of the ovary.

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Anti-CDC25B Rabbit Polyclonal Antibody

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Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein.

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G proteins mediate a number of cellular processes. The protein encoded by this gene belongs to the RGS (regulators of G protein signaling) family and specifically interacts with G protein, GAI3. This protein is a guanosine triphosphatase activating protein that functions to down regulate Galpha i/Galpha q linked signaling.

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Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci (By similarity). The CCR4-NOT complex functions as general transcription regulation complex. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene.

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The protein arginine deiminase (PAD) family of proteins, often referred to as peptidylarginine deiminases, catalyze the deimination of arginine residues of proteins. In the presence of calcium, the proteins in the PAD family act as catalysts for the posttranslational modification reaction that converts methylarginine to citrulline. The PAD proteins are cytoplasmic proteins primarily detected in eosinophils and neutrophils. The only tissue that contains all four forms of PAD (PADI1-4) is epidermis. PADI2 may play a crucial role during terminal differentiation of epidermal keratinocytes.