"Bioss"

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EF-1 (elongation factor-1) is a multi-protein complex that is responsible for the delivery of aminoacyl-tRNAs to the ribosome. EF-1 gamma (elongation factor 1-gamma), also known as EEF1G or GIG35, is a 437 amino acid subunit of the EF-1 complex. Expressed in stomach, pancreas, brain, lung, kidney, intestine, liver and spleen, EF-1 gamma contains an N-terminal glutathione transferase domain which is thought to be involved in anchoring the complex to various cellular components. Additionally, EF-1 gamma may play a key role in the assembly of multiprotein complexes containing aminoacyl-tRNA synthetases. Increased expression of EF-1 gamma is associated with pancreatic cancer, suggesting a possible role for EF-1 gamma in the oncogenic transformation process.

Supplier: Bioss

This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling.

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Centromeric histone H3-like protein-2

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Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyses the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Beta-hexosaminidase is composed of two subunits, alpha and beta, which are encoded by separate genes. Both beta-hexosaminidase alpha and beta subunits are members of family 20 of glycosyl hydrolases. Mutations in the alpha or beta subunit genes lead to an accumulation of GM2 ganglioside in neurons and neurodegenerative disorders termed the GM2 gangliosidoses. Beta subunit gene mutations lead to Sandhoff disease (GM2-gangliosidosis type II).

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Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

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Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG. Prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis.

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Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).

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This gene encodes a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. These proteins are synthesized as prepropeptides, cleaved, and then processed into dimeric proteins. This protein may act as an important signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. This gene is differentially regulated during the formation of various tumors. [provided by RefSeq, Jul 2008].

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Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.

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DENND4C is a 1,673 amino acid multi-pass membrane protein. DENND4C contains a dDENN domain, DENN domain, uDENN domain and a PPR (pentatricopeptide) repeat. As a result of alternative splicing, six DENND4C isoforms exist. The gene encoding DENND4C maps to human chromosome 9, which houses over 900 genes and comprises nearly 4% of the human genome. Hereditary hemorrhagic telangiectasia, which is characterized by harmful vascular defects, and Familial dysautonomia, are both associated with chromosome 9. Notably, chromosome 9 encompasses the largest interferon family gene cluster.

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NSP type 5 alpha 3 alpha is a novel structure protein belonging to the cytospin-A family, that may play a role in nuclear function during cell division. It is also highly expressed in certain tumor cell lines, suggesting that it may serve as a good tumor marker. It was was cloned as part of a chromosomal translocation involving PDGFRB in a case of juvenile myelomonocytic leukemia.

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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. Zinc finger protein 568 (ZNF568) is a 644 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF568 contains fifteen C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF568 exist as a result of alternative splicing events.

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ADAR1 converts adenosine to inosine in dsRNA, which destabilizes the dsRNA helix. This activity is important for various functions like site-specific RNA editing of transcripts of the glutamate receptors and modifying viral RNA genomes (which may be responsible for hypermutation of certain negative-stranded viruses, e.g., measles virus). ADAR1 also binds to short interfering RNAs (siRNA) without editing them and suppresses siRNA-mediated RNA interference. This protein is ubiquitously expressed, with the highest levels being found in brain and lung.

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CC85C.

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CCR7 is a member of the G protein coupled receptor family (subfamily : chemokine). This receptor was identified as a gene induced by the Epstein Barr virus (EBV), and is thought to be a mediator of EBV effects on B lymphocytes. CCR7 has been reported to be expressed in blood, bone marrow, lymph node, and intestine. It is particularly expressed in lymphoid tissues and in activated B and T lymphocytes and has been shown to control the migration of memory T cells to inflamed tissues, as well as stimulate dendritic cell maturation. The chemokine (C-C motif) ligand 19 (CCL19/ECL) has been reported to be a specific ligand of this receptor. ESTs have been isolated from blood, embryo, lymph node, and thymus libraries.

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NBL1 (Neuroblastoma, suppression of tumorigenicity 1) is a candidate tumor suppressor of neuroblastoma and may play a role in preventing cells from entering the final stage (G1/S) of the transformation process. NBL1 is a member of the evolutionarily conserved CAN (Cerberus and DAN) family of proteins, which contain a domain resembling the CTCK (C-terminal cystine knot-like) motif found in a number of signaling molecules. It is a member of a class of glycoproteins shown to be secreted inhibitors of the transforming growth factor-beta (TGF-beta) and bone morphogenic protein pathways.