127976 Results for: "Bioss"

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Anti-Brain1/POU3F3 Rabbit Polyclonal Antibody

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Anti-SPOCK1 Rabbit Polyclonal Antibody

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RILPL2 is a 211 amino acid protein that belongs to the RILPL family. RILPL2 does not regulate lysosomal morphology or distribution. RILPL2 shares 32% and 18% amino acid identity with RILPL1 and RILP, respectively. RILPL2 as a novel interacting partner for the actin-based molecular motor MyoVa, and has a novel role for RILPL2 in controlling neuronal morphogenesis. It has been suggested that there is also a novel role for RILPL2 in the regulation of cellular shape and dendritic-spine morphogenesis, probably via the Rac1-Pak pathway. PCR analysis of human tissues detects highest RILPL2 expression in lung, followed by placenta. Lower expression is detected in liver, kidney, pancreas, heart and brain, but no expression is detected in skeletal muscle. The RILPL2 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, and maps to human chromosome 12q24.31.

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Myo-inositol is involved in many important aspects of cellular regulation including membrane structure, signal transduction and osmoregulation. It is taken up into cells by the sodium/myo-inositol cotransporter (SMIT). SMIT activity maintains intracellular concentrations of myo-inositol; it is upregulated in response to hypertonic stress. The human SMIT protein is encoded by the SLC5A3 gene, which maps to chromosome 21q22.12. It is expressed in many human tissues, such as brain, kidney and placenta. Specifically, SMIT is abundantly expressed throughout the whole brain and spinal cord in fetal rat, but is downregulated in adult rat brain with the exception of the choroid plexus, where SMIT expression remains high. In kidney, SMIT localizes to the baso-lateral membranes of the thick ascending limb of Henle (TAL) and the inner medullary collecting duct (IMCD). Impaired SMIT activity is implicated in the pathogenesis of diabetes and Down syndrome.

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There are three SorCS genes that have diverse, partially overlapping functions in the central nervous system. In the developing and mature central nervous system, SorCS1, SorCS2 and SorCS3 genes are expressed in a combinatorial, non-overlapping pattern. SorCS proteins show homology to the mosaic receptor SorLA and the neurotensin receptor sortilin, based on a common VPS10 domain, which is the hallmark of the SorCS receptor family. SorCS2 (sortilin-related VPS10 domain containing receptor 2) is a 1,150 amino acid single-pass type I membrane protein that is highly expressed in brain and kidney. Containing six BNR repeats and a single PKD domain, SorCS2 is encoded by a gene that maps to human chromosome 4, which encodes nearly 6% of the human genome and has the largest gene deserts (regions of the genome with no protein encoding genes) of all of the human chromosomes.

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The ADP-ribosylation factor (Arf) family comprises a group of structurally and functionally conserved 21 kDa proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. Arf is involved in intracellular protein traffic to and within the Golgi complex. Arf has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. Like other small GTPases, Arf is found to be active when bound to GTP and inactive when bound to GDP. Arf’s activation is dependent upon guanine nucleotide exchange factors (GEFs) which increase the rate of exchange of bound GDP with GTP. All GEFs have a highly conserved Sec7 domain. GEF activity lies in the Sec7 domain and this activity has been shown to be inhibited by the fungal metabolite brefeldin-A (BFA). A small group of GEFs which are insensitive to brefeldin-A (BFA) include cytohesin-1 (B2-1), cytohesin-2 (ARNO), cytohesin-3 (ARNO3), and cytohesin-4. All cytohesins function in the cell periphery and contain a pleckstrin homology (PH) domain. The PH domain has been shown to interact with phosphatidylinositol 3,4,5-triphosphate and is believed to promote membrane targeting of the cytohesins. Recruitment of the cytohesins to the membranes can occur in response to tyrosine kinase receptor activation. This response appears to require the activation of phosphatidylinositol 3-kinase (PI 3-kinase).

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This gene is a member of the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. The product of this gene typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. This protein plays a role in maintaining cellular structural integrity and also functions in signal transduction and cellular differentiation. Mutations in this gene cause cryptogenic cirrhosis. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2012].

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When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.

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Anti-FOG2 Rabbit Polyclonal Antibody

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Carbonic anhydrases are a large family of zincmetalloenzymes that catalyze the reversible hydration of carbondioxide. They participate in a variety of biological processes,including respiration, calcification, acid-base balance, boneresorption, and the formation of aqueous humor, cerebrospinalfluid, saliva, and gastric acid. They show extensive diversity intissue distribution and in their subcellular localization. Thecytosolic protein encoded by this gene is predominantly expressedin the salivary glands. Alternative splicing in the coding regionresults in multiple transcript variants encoding differentisoforms. [provided by RefSeq, Jul 2008].

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This gene encodes a protein that appears to play a role in nuclear envelope integrity, possibly related to microtubule attachments. Mutations in this gene cause congenital dyserythropoietic anemia type I, a disease resulting in morphological and functional abnormalities of erythropoiesis.

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Ankyrin repeats containing cofactors may recruit histone deacetylases to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation.

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Anti-ANKRD13A Rabbit Polyclonal Antibody

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APOL3 may be involved in cytoplasmic lipid transport or allow the binding of lipids to organelles. It is widely expressed; the highest levels are in prostate, lung and placenta; also detected in kidney, bone marrow, spleen, thymus, spinal cord, adrenal gland, salivary gland, trachea and mammary gland; levels are low in brain, heart, fetal liver, pancreas and testis. There are three named isoforms.

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CLN6, a 311 amino acid protein, has seven predicted transmembrane domains and is conserved across vertebrates. The CLN6 protein localizes to the endoplasmic reticulum but contributes to lysosomal function. Mutations in the CLN6 gene cause variant late-onset infantile neuronal ceroid lipofuscinosis (vLINCL), a lysosomal storage disorder marked by progressive mental deterioration and blindness; part of a group of severe inherited neurodegenerative disorders affecting children wherein lysosomes accumulate storage material, causing the death of neurons. CLN6 is one of eight proteins, including CLN1-8, that are associated with NCL.

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FBXO4 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It probably recognizes and binds to phosphorylated target proteins. It recognizes TERF1 and promotes its ubiquitination together with UBE2D1.

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Anti-NPSR1 Rabbit Polyclonal Antibody

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Anti-ARNTL2 Rabbit Polyclonal Antibody

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Anti-ABLIM1 Rabbit Polyclonal Antibody

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Anti-AGRP Rabbit Polyclonal Antibody

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Required for depolarization-dependent survival of cultured cerebellar granule neurons. May mediate homophilic as well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May contribute to signal transduction through its intracellular domain. May be required for tumorigenesis of a subset of gastric adenocarcinomas.

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In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

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Participates in the synthesis of thyroid hormones. Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage.

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Anti-NMUR2 Rabbit Polyclonal Antibody

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Anti-HSPB2 Rabbit Polyclonal Antibody

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No data available.

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Contributes to degradation of proteins cross-linked by transglutaminases. Degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. Catalyzes the formation of 5-oxoproline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine.

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AADACL3 is a 350 amino acid protein that belongs to the 'GDXG' lipolytic enzyme family and participates in hydrolase activity. Existing as two alternatively spliced isoforms, AADACL3 is encoded by a gene that maps to human chromosome 1p36.21. Chromosome 1, the largest human chromosome, makes up 8% of the human genome and contains about 260 million base pairs, which encode 3,000 genes. Chromosome 1 houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome. Aberrations in chromosome 1 are found in a variety of cancers, including head and neck cancer, malignant melanoma and multiple myeloma.

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Alpha-aminoadipic semialdehyde synthase (AASS), also designated lysine ketoglutarate reductase (LKR) or saccharopine dehydrogenase (SDH), is a 926 amino acid protein that exists as a homodimer in the mitochondria. AASS acts as a bifunctional enzyme containing the lysine alpha-ketoglutarate reductase (LKR) and saccharopine dehydrogenase activities that catalyzes the first two steps in lysine degradation. It is widely expressed with highest expression in liver and transcription of the AASS gene is induced upon starvation. Mutations in the gene encoding AASS result in various forms familial hyperlysinemias (FH), autosomal recessive disorders characterized by hyperlysinemia, lysinuria, and variable saccharopinuria. However, no adverse mental or physical effects have been found in patients with hyperlysinemia.

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Gonadotropin-releasing hormone (GnRH) is released in a pulsatile manner that varies with the reproductive cycle. This hypothalamic hormone is transported to the pituitary, where it binds to specific receptors and regulates the synthesis and release of luteinizing hormone (LH) and follicle-stimulating hormone (FSH). Localized to the cell membrane, GnRHR2 mediates its own receptor activity via association with G proteins, thereby activating a phosphatidylinositol-calcium second messenger system that regulates GnRHR2 function. GnRHR2 is thought to have potent antiproliferative effects on ovarian and endometrial cancer cells, suggesting a possible role in tumor suppression. Due to alternative splicing events, GnRHR2 is expressed as two isoforms.