42864 Results for: "ProSci Inc."

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CUL5 encodes a protein that is involved in the regulation of cellular growth and promotes vif ubiquination.

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CD55 is a member of the RCA (regulators of complement activation) family. RCA proteins is characterized by the presence of four to 30 SCRs (short consensus repeats also called CCPs for control protein modules) in their plasmaexposed regions. CD55 containing four SCR modules is involved in the regulation of the complement cascade. CD55 is known to bind CD97 via the first SCR. It also binds physiologically generated C3 convertases with its second and third SCRs. Binding results in an accelerated “decay”, or dissociation of active C3 convertases, thus blocking the development of C’ attack complexes on nonforeign cells. It is known that viruses and bacteria also utilize multiple SCR sites for infection.

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Receptors for the Fc region of IgG (Fc gamma R) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Human Fc gamma Rs are divided into three classes designated Fc gamma RI (CD64), Fc gamma RII (CD32), and Fc gamma RIII (CD16), which generate multiple isoforms, are recognized. The activating­ type receptor either has or associates non­covalently with an accessory subunit that has an immunoreceptor tyrosine­based activation motif (ITAM) in its cytoplasmic domain. Fc gamma RI binds IgG with high affinity and functions during early immune responses, whereas Fc gamma RII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. Three genes for human Fc gamma RII (A, B, and C) and one for mouse (Fc gamma RIIB), encoding type I transmembrane proteins with ITAM motifs (Fc gamma RII A and C) or ITIM motifs (Fc gamma RIIB) in their cytoplasmic domains, have been identified. Human CD32, also known as Low affinity immunoglobulin gamma Fc region receptor II-a (IgG Fc receptor II-a), Fc gamma RII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcR gamma , CD32a (Fc gamma RII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fc gamma RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors.

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Tumor Necrosis Factor Receptor Superfamily Member 21 (TNFRSF21) is a type I transmembrane receptor that includes four extracellular cysteine-rich motifs and a cytoplasmic death domain. DR6 is highly expressed in heart, brain, placenta, pancreas, lymph node, thymus and prostate. DR6 may activate NF-kappa-B and JNK to promote apoptosis and T-cell differentiation. In addition, DR6 binds with N-APP, which is released by the deprivation of Trophic-factor. It triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). DR6 is also expressed on the tumor cell lines and can be induced by TNF- alpha.

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Interferon gamma receptor 1 (IFNGR1) is also known as CD antigen CD119, which belongs to the type II cytokine receptor family. IFNGR1 contains two fibronectin type-III domains and two Ig-like C2-type (immunoglobulin-like) domains. IFNGR1 / CD119 is receptor for interferon gamma. Two receptors bind one interferon gamma (IFNG) dimer.

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Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle materials when they are no longer needed. Cathepsin A interacts with the enzymes beta -galactosidase and neuraminidase 1, which play a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) or fats (glycolipids). Cathepsin A forms a complex with these two enzymes and directs their transport within the cell to the lysosomes. Within lysosomes, cathepsin A activates the enzymes and prevents their breakdown.

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FAM121B belongs to the FAM121 family and the function remains unknown.

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Sm-like proteins were identified in a variety of organisms based on sequence homology with the Sm protein family. Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.Sm-like proteins were identified in a variety of organisms based on sequence homology with the Sm protein family (see SNRPD2; MIM 601061). Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.

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In mammals, the Y chromosome directs the development of the testes and plays an important role in spermatogenesis. A high percentage of infertile men have deletions that map to regions of the Y chromosome. The DAZ (deleted in azoospermia) gene cluster maps to the AZFc region of the Y chromosome and is deleted in many azoospermic and severely oligospermic men. It is thought that the DAZ gene cluster arose from the transposition, amplification, and pruning of the ancestral autosomal gene DAZL also involved in germ cell development and gametogenesis. DAZAP1 is a RNA-binding protein with two RNP motifs that was originally identified by its interaction with the infertility factors DAZ and DAZL.In mammals, the Y chromosome directs the development of the testes and plays an important role in spermatogenesis. A high percentage of infertile men have deletions that map to regions of the Y chromosome. The DAZ (deleted in azoospermia) gene cluster maps to the AZFc region of the Y chromosome and is deleted in many azoospermic and severely oligospermic men. It is thought that the DAZ gene cluster arose from the transposition, amplification, and pruning of the ancestral autosomal gene DAZL also involved in germ cell development and gametogenesis. This gene encodes a RNA-binding protein with two RNP motifs that was originally identified by its interaction with the infertility factors DAZ and DAZL. Two isoforms are encoded by transcript variants of this gene.In mammals, the Y chromosome directs the development of the testes and plays an important role in spermatogenesis. A high percentage of infertile men have deletions that map to regions of the Y chromosome. The DAZ (deleted in azoospermia) gene cluster maps to the AZFc region of the Y chromosome and is deleted in many azoospermic and severely oligospermic men. It is thought that the DAZ gene cluster arose from the transposition, amplification, and pruning of the ancestral autosomal gene DAZL also involved in germ cell development and gametogenesis. This gene encodes a RNA-binding protein with two RNP motifs that was originally identified by its interaction with the infertility factors DAZ and DAZL. Two isoforms are encoded by transcript variants of this gene.

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Mucin-15 is a single-pass type I membrane protein member of the Mucin family. Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most metazoans. A key characteristic of Mucins is their ability to form gels. Therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. Mucin-15 is expressed in many tissues. Mucin-15 is highly glycosylated (N- and O-linked carbohydrates). Mucin-15 may play a role in the cell adhesion to the extracellular matrix.

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CSGlcA-T belongs to the chondroitin N-acetylgalactosaminyltransferase family. It transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. CSGlcA-T has no N-acetylgalactosaminyltransferase activity.

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GA Binding Protein. chain (GABP-. subunit, GABPA, nuclear respiratory factor-2 subunit. transcription factor E4TF1-60) is one of three GA-binding protein transcription factor subunits which functions as a DNA-binding subunit. Since this subunit shares identity with a subunit encoding the nuclear respiratory factor 2 gene, it is likely involved in activation of cytochrome oxidase expression and nuclear control of mitochondrial function. This subunit also shares identity with a subunit constituting the transcription factor E4TF1, responsible for expression of the adenovirus E4 gene. Because of its chromosomal localization and ability to form heterodimers with other polypeptides, this gene may play a role in the Down Syndrome phenotype.

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Serpin Peptidase Inhibitor, Clade A, Member 6 (SerpinA6) belongs to the Serine Protease Inhibitors superfamily. SerpinA6 is synthesized in liver and has also been identified in a number of glycocorticoid responsive cells. SerpinA6 has an alpha-globulin protein with corticosteroid-binding properties. It is the major transport protein for glucocorticoids and progestins in the blood of most vertebrates. Defects in SERPINA6 are a cause of corticosteroid-binding globulin deficiency which is an extremely rare hereditary disorder characterized by reduced corticosteroid-binding capacity with normal or low plasma corticosteroid-binding globulin concentration, and normal or low basal cortisol levels associated with hypo/hypertension and muscle fatigue.

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Anti-FEZ1 Goat Polyclonal Antibody

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Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.

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Interferon alpha-6 (IFN- alpha6) is a secreted protein which belongs to the alpha/ beta interferon family. IFN- alpha6 is produced by macrophages, expressed at low level, only 1.0% of the average gene in this release. IFN- alpha6 contains interferon alpha, beta and delta domain. IFN- alpha has antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.

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Anti-F13A1 Goat Polyclonal Antibody

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Anti-FNBP1 Goat Polyclonal Antibody

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Proteinase-3 is a neutral serine proteinase that belongs to the peptidase S1 family and Elastase subfamily. It contains one peptidase S1 domain and it is expressed mainly in neutrophil granulocytes. The primary function of Proteinase-3 is thought to be degradation of extracellular proteins at sites of inflammation, but excessive or prolonged proteolytic activity may cause harmful effects in the body. It is the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the cANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease Wegener's granulomatosis.

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PCDH15 is a member of the cadherin superfamily. Family members encode integral membrane proteins that mediate calcium-dependent cell-cell adhesion. PCDH15 consists of a signal peptide, 11 extracellular calcium-binding domains, a transmembrane domain and a unique cytoplasmic domain. It plays an essential role in maintenance of normal retinal and cochlear function. Mutations in this gene have been associated with hearing loss, which is consistent with its location at the Usher syndrome type 1F (USH1F) critical region on chromosome 10.

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Clusterin shares homology with the small heat shock protein family of molecular chaperones. The mature secreted form of the protein is a glycosylated, 80-kDa disulfide-linked heterodimer of alpha and beta subunits (produced by internal cleavage). Clusterin is expressed in virtually all tissues and found in all human fluids. It is involved in numerous physiological processes important for carcinogenesis and tumor growth, including apoptotic cell death, cell cycle regulation, DNA repair, cell adhesion, tissue remodeling, lipid transportation, membrane recycling, and immune system regulation. Clusterin also exists as a nuclear protein. The secreted form of Clusterin has extracellular chaperone and anti-apoptotic activities while the nuclear form acts as a proapoptotic factor.

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Granulins have possible cytokine-like activity. They are important in normal development, inflammation, wound repair, and tumorigenesis.

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PSG2 is a secreted protein that in humans is encoded by the PSG2 gene. It is a member of the human pregnancy-specific glycoproteins (PSGs) family. These proteins are synthesised in large amounts by placental trophoblasts and released into the maternal circulation during pregnancy. PSG2 consist of a single N domain, with structural similarity to the immunoglobulin variable domains, followed by a variable number of immunoglobulin constant-like A and/or B domains. It has an arg-gly-asp (RGD) motif, which has been shown to function as an adhesion recognition signal for several integrins, in the N-terminal domain.

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ARG1 is a member of the ureohydrolase family of enzymes. ARG1 can catalyse the hydrolysis of arginine to ornithine and urea. In the urea cycle, ARG1 catalyses the fifth and final step, a series of biochemical reactions in mammals during which the body disposes of harmful ammonia. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterised by hyperammonemia.

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MGMT belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. MGMT involved in the cellular defense against the biological effects of O6-methylguanine in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. MGMT catalyses the chemical reaction: DNA (containing 6-O-methylguanine) and proteinL-cysteine into DNA (without 6-O-methylguanine) and protein S-methyl-L-cysteine.

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NHP2 belongs to the H/ACA snoRNPs gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been organised into 2 families: C/D and H/ACA. NHP2 forms a small ribonucleoprotein particle with GAR1 (NOLA1). NHP2 is involved in a variety of aspects of rRNA processing and modification. NHP2 localises to the dense fibrillar component of the nucleolus and in nuclear Cajal bodies. NHP2 may also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.

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ZNF276 is a new candidate transcription factor

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The NS3 serine protease, in association with NS4A, is responsible for the cleavages of the Hepatitis C virus protease complexes NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Hepatitis C virus protease NS3-NS4A colocalizes with IPS-1/VISA/MAVS/Cardif in the mitochondrial membrane and has been shown to cleave the TLR3 adapter TRIF and Cardif to eliminate the antiviral signaling pathways. NS3-NS4A represents an important target for anti-HCV drugs.

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GPxs are glutathione peroxidases involved in balancing the H2O2 homeostasis in signaling cascades. GPxs have been known to catalyze the reduction of H2O2 or organic hydroperoxides to water or the corresponding alcohols, respectively, typically using glutathione (GSH) as reductant. GPx8 (probable glutathione peroxidase 8) is a 209-aa, 24kDa protein with an N-terminal cytosolic tip, a predicted transmembrane segment and a catalytic domain located in the endoplasmic reticulum (ER) lumen. GPx8 is a CysGPxs with low glutathione peroxidase activity. A recent study identified GPx8 as a cellular substrate of the hepatitis C virus NS3-4A protease. GPx8 cleavage by NS3-4A occurs at Cys11, removing the cytosolic tip of GPx8 and was observed in different experimental systems as well as in liver biopsies from patients with chronic hepatitis C.

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Beta-casein is a protein that in humans is encoded by the CSN2 gene.Beta-casein is a 226 amino acids protein that belongs to the beta-casein family.It is secreted in milk. Beta-casein palys important role in determination of the surface properties of the casein micelles.