381450 Results for: "single-use assemblies"

Supplier: Genetex

Gastric Inhibitory Polypeptide Receptor is a member of the G protein-coupled receptor (GPCR, or GPR) family (subfamily Gastric inhibitory polypeptide). Members of this family contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins. Gastric inhibitory polypeptide receptor is a receptor for gastric inhibitory polypeptide (GIP), this is a 42-amino acid polypeptide synthesized by K cells of the duodenum and small intestine. It was originally identified as an activity in gut extracts that inhibited gastric acid secretion and gastrin release, but subsequently was demonstrated to stimulate insulin release potently in the presence of elevated glucose. The insulinotropic effect on pancreatic islet beta-cells was then recognized to be the principal physiologic action of GIP. Together with glucagon-like peptide-1, GIP is largely responsible for the secretion of insulin after eating. It is involved in several other facets of the anabolic response. GIPR expression has been reported in human bone, fetal adrenal, and pancreas. Little expression has been identified in normal adult adrenal, but overexpression of GIPR has been observed in the adrenal in food-dependent Cushing's syndrome. GIPR expression has been identified in rat brain, heart, pancreas, and small intestine. ESTs have been isolated from colon libraries.

Supplier: Prosci

Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA. On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.

Supplier: Zymo Research

Automation-specific streamlined design for high-throughput bisulfite conversion of DNA for methylation analysis.

Supplier: Prosci

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. 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. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. PSME3 is the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring.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. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.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. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.

Supplier: 3M Healthcare

3M™ Water Filtration Products High Flow Series Model CARTPAK SF165 Replacement Cartridge Kit provides Recipe Quality Water™ that reduces sediment*, chlorine taste and odor, and scale* for boiler based steamers, combi and proofer ovens. Our cartpak simplifies ordering of replacement cartridges for the SF165 system.

Supplier: BioVendor

Visceral adipose tissue – derived serpin A12 (vaspin), also named OL-64, an adipocytokine, is structurally a member of the serine protease family. Serpins are the most diverse family of protease inhibitors. Their typical structural feature is the core domain composed from 3 beta-sheets and 9 alpha-helixes. The inhibitory activity of vaspin has not been described up to now, but its reactive site loop is typical for this proteinase family. Human Vaspin protein is composed of 395 amino acids and has a molecular weight of approximately 45.2 kDa and predicted pI 9.26. The cDNA was first isolated from white adipose tissue of Otsuka Long-Evans Tokushima Fatty (OLETF) rats. Vaspin mRNA expression is specific for visceral adipose tissues and it is also found circulating in the serum. The level of serum vaspin increased with age up to the peak of obesity, body weight and insulin resistance in OLETF rats and decreases with worsening of diabetes. Vaspin expression is missing in the diabetes-resistant lean rats, LETO, in comparison to OLEFT rats, animal model of metabolic syndrome. Expression was also absent in the subdermal, brown fatty tissue and other non-adipose tissues in OLEFT rats. These findings lead to the conclusion that the target tissue for insulin sensitising effect of vaspin is white adipose tissue. In humans, elevated serum concentration of vaspin is associated with obesity and impaired insulin sensitivity.

Supplier: Biosensis

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

Supplier: Rockland Immunochemical

A novel cytokine, designated IL-TIF for IL-10 related T cell-derived inducible factor and IL-22, was recently identified. The receptor for IL-22 (IL-22R, also termed CRF2-9 and IL-TIF-R1 chain) is a new member of the class II cytokine receptor family. IL-22R forms a complex with IL-10 receptor beta chain and mediates IL-22 signaling. IL-22 and its receptor activate JAK-STAT signaling pathway. IL22R is expressed in normal liver and kidney and their cell lines HepG2 and TK-10. A soluble form of IL-22 receptor, also termed IL-22 binding protein (IL-22BP) and IL-22 receptor-alpha 2 (IL-22RA2), was identified very recently. IL-22BP prevents binding of IL-22 to the functional cell surface IL-22R complex and neutralizes IL-22 activity. LPS induces IL-22 expression, which indicates the role of IL-22 in inflammatory response.

Supplier: Rockland Immunochemical

Anti-Monkey IgG (gamma chain) DyLight™488 conjugated antibody generated in goat detects specifically monkey IgG (gamma chain). Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. IgG binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsinization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. This DyLight™488 conjugated anti-Monkey IgG gamma chain secondary antibody is ideal for investigators who routinely perform ELISA, Sandwich ELISA, titration assays, western-blot, immunoprecipitation and more general immunoassays. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment.

Supplier: Prosci

This antibody recognizes a protein of 56kDa, identified as cytokeratin 6 (CK6) or Keratin 6. In humans, multiple isoforms of Cytokeratin 6 (6A-6F), encoded by several highly homologous genes, have distinct tissue expression patterns, and Cytokeratin 6A is the dominant form in epithelial tissue. The gene encoding human Cytokeratin 6A maps to chromosome 12q13, and mutations in this gene are linked to several inheritable hair and skin pathologies. Keratins 6 and 16 are expressed in keratinocytes, which are undergoing rapid turnover in the suprabasal region (also known as hyper-proliferation-related keratins). Cytokeratin 6 is found in hair follicles, suprabasal cells of a variety of internal stratified epithelia, in epidermis, in both normal and hyper-proliferative situations. Epidermal injury results in activation of keratinocytes, which express Cytokeratin 6 and 16. Keratin 6 is strongly expressed in about 75% of head and neck squamous cell carcinomas. Expression of Cytokeratin 6 is particularly associated with differentiation.

Supplier: Genetex

ATF2 (Activating Transcription Factor 2, CRE-BP, HB16, CREB2, TREB7) is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with c-Jun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full-length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy-terminal DNA-binding domain with the amino-terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: G-Biosciences

G-Biosciences' Yeast Geno-DNA-Template™ extraction kit isolates high quality genomic DNA from yeast cultures

Supplier: Rockland Immunochemical

Interleukin-33 (IL-33) is a recently identified member of the IL-1 family of cytokines whose other members include IL-1ab, IL-1Ra and IL-18. Its receptor has been shown to be ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling and IL-1R accessory protein (IL-1RAcP). Receptor binding of IL-33 activates NF-kB and MAP kinases and induces the expression of TH2-associated cytokines such as IL-4, IL-5 and IL-6. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine. Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties. Despite its predicted molecular weight, IL-33 will often run at higher molecular weight in SDS-PAGE.

Supplier: Prosci

The Cell-division cycle protein 20 is an essential regulator of cell division that is encoded by the CDC20 gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/C-Cdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle.

Cdc20 appears to act as a regulatory protein interacting with many other proteins at multiple points in the cell cycle. It is required for two microtubule-dependent processes: nuclear movement prior to anaphase, and chromosome separation. [Wiki]

Supplier: Prosci

The protein encoded by this gene belongs to the DEAD-like helicase superfamily, and shares similarity with Saccharomyces cerevisiae Rad54, a protein known to be involved in the homologous recombination and repair of DNA. This protein has been shown to play a role in homologous recombination related repair of DNA double-strand breaks. The binding of this protein to double-strand DNA induces a DNA topological change, which is thought to facilitate homologous DNA paring, and stimulate DNA recombination. The protein encoded by this gene contains an ATPase/helicase domain, and thus it belongs to the SWI/SNF family of chromatin remodeling proteins. The mutations of this gene are associated with an X-linked mental retardation (XLMR) syndrome most often accompanied by alpha-thalassemia (ATRX) syndrome. These mutations have been shown to cause diverse changes in the pattern of DNA methylation, which may provide a link between chromatin remodeling, DNA methylation, and gene expression in developmental processes. This protein is found to undergo cell cycle-dependent phosphorylation, which regulates its nuclear matrix and chromatin association, and suggests its involvement in the gene regulation at interphase and chromosomal segregation in mitosis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Rockland Immunochemical

The pro-inflammatory cytokine IL-1 induced cellular response requires IL-1 receptor complex including IL-1RI and IL-1RAcP. MyD88 has been identified as an adapter molecule in the IL-1 signaling pathway. MyD88 associates with and recruits IRAK to the IL-1 receptor complex in response to IL-1 treatment and dominant negative form of MyD88 attenuates IL-1R-mediated NF-kB activation. MyD88 is also employed as a regulator molecule by IL-18 receptor and human Toll receptor, which are members in the Toll/IL-1R family of receptors. Targeted disruption of the MyD88 gene results in lose of cellular responses to IL-1 and IL-18, and MyD88-deficient mice lack responses to bacterial product LPS that employs Toll-like receptors 2 and 4 (TLR2 and TLR4) as the signaling receptors. MyD88 is a general adapter protein for the Toll/IL-1R family of receptors and plays an important role in the inflammatory response induced by cytokines IL-1 and IL-18 and endotoxin. MyD88 gene is expressed in many tissues.

Supplier: Rockland Immunochemical

Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer's disease. In addition to PEN2, nicastrin and APH-1, Presenilin1 forms the gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease. Multiple isoforms of presenilin1 are known to exist. This antibody has no cross-reactivity to presenilin2.

Supplier: Prosci

Tyrosine-protein kinase ZAP70 is a tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, it phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. [UniProt]

Supplier: Biosensis

FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer composed of two large adaptins (gamma1/AP1G1 or gamma2/AP1G2 and beta1A/AP1B1 or beta1B/AP1B1), a medium adaptin (mu1A/AP1M1 or mu1B/AP1M2) and a small adaptin (sigma1A/AP1S1 or sigma1B/AP1S2 or sigma1C/AP1S3). SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle; cytoplasmic vesicle membrane; peripheral membrane protein; cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed. DISEASE: Deletion of the AP1B1 gene may play a role in the tumorigenesis of meningiomas. SIMILARITY: Belongs to the adaptor complexes large subunit family.

Supplier: MICROBIOLOGICS, INC.

EZ-Accu Shot™ Select boasts all the same features and benefits as the original EZ-Accu Shot™, but includes six compendial QC microorganism strains for Growth Promotion Testing in one convenient package. EZ-Accu Shot™ Select lyophilized QC microorganism preparations are designed to deliver 10-100 CFU per 0.1 mL of hydrated suspension as recommended by the USP/JP/Ph. Eur. With little to no preparation time required and up to eight hours of stability, EZ-Accu Shot™ Select adds efficiency and flexibility to QC laboratories’ busy schedules. Each 1.2 mL vial of hydrated suspension offers 10 inocula. For added convenience, individual peel-off informational labels are included for each strain.

Supplier: INDIGO BIOSCIENCES INC MS

Eliminate weeks of cell culture while achieving superior sensitivity with reproducible results from this all-inclusive cell-based luciferase reporter assay. INDIGO’s Human ER Reporter Assays Panel All-inclusive Cell-Based Luciferase Reporter Assay Kit includes reporter cells for each ER, optimized cell culture medium, a medium for diluting test compounds, 17-β-estradiol control agonist, stable-glow luciferase detection reagent, detailed protocol, protocol quick guide, and a cell culture-ready assay plate in strip-well format.

Supplier: Prosci

ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

Supplier: Prosci

Rb operates in the midst of the cell cycle clock apparatus. Its main role is to act as a signal transducer connecting the cell cycle clock with the transcriptional machinery. It plays an important role in the Rb/ E2F pathway in cell proliferation, cell fate determination, and cancer. Cellular senescence is a stable form of cell cycle arrest that limits proliferation of damaged cells and act as a natural barrier to cancer progression. A distinct heterochromatic structure that accumulates in senescent human fibroblasts, designated as SAHF (Senescence-Associated Heterochromatic Foci). SAHF formation coincides with recruitment of heterochromatin proteins and the Rb protein to E2F-responsive promoters and is associated with the stable repression of E2F target genes. Both SAHF formation and the silencing of E2F target genes depended on the integrity of the Rb pathway and do not occur in reversibly arrested cells. Rb activates transcription of the c-Jun gene through the SP1-binding site within the c-Jun promoter

Supplier: Prosci

Interleukin-27 (IL-27) is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines. It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the cloned 28 kDa glycoprotein that is related to the p35 chain of IL-12. IL-27 is expressed by monocytes, endothelial cells and dendritic cells. IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1. IL-27 has both anti- and proinflammatory properties. As an antiinflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity. At the onset of infection, IL-27 induces an IL-12 receptor on naie CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development). Notably, IL-12 family cytokines are both induced and inhibited by bacterial products. Microbes promote IL-27 secretion through TLR4, and also block IL-27 production via C5a induction.

Supplier: Rockland Immunochemical

SLC22A6(Solute carrier family 22 (organic anion transporter), member 6), also called OAT1 or PAHT, is a protein that in humans is encoded by the SLC22A6 gene, which is also a member of the organic anion transporter (OAT) family of proteins. OAT1 is a transmembrane protein that is expressed in the brain, the placenta, the eyes, smooth muscles, and the basolateral membrane of proximal tubular cells of the kidneys. The SLC22A6 gene is mapped on 11q12.3. It plays a central role in renal organic anion transport. Along with OAT3, OAT1 mediates the uptake of a wide range of relatively small and hydrophilic organic anions from plasma into the cytoplasm of the proximal tubular cells of the kidneys. The SLC22A6 gene contains 10 exons and spans 8.2 kb. OAT1 functions as organic anion exchanger. When the uptake of one molecule of an organic anion is transported into a cell by an OAT1 exchanger, one molecule of an endogenous dicarboxylic acid (such as glutarate, ketoglutarate, etc) is simultaneously transported out of the cell. PAH uptake in Xenopus oocytes injected with OAT1 mRNA was demonstrated by Race et al. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

Nicastrin, in addition to presenilin, PEN2, and APH-1 forms the gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease. Nicastrin is also thought to be involved in cell proliferation and signaling, especially in regards to activation of Notch receptors as loss of Nicastrin expression results in mouse embryonic lethality.

Supplier: Rockland Immunochemical

Movement of lymphocytes through lymphoid organs is required for generating immunity. Their migration into lymph nodes follows a series of events including integrin activation through chemokine signaling, adhesion and diapedis. The release of lymphocytes from lymph nodes is regulated by the phospholipid sphingosine-1-phosphate (S1P). One of its receptors S1P1 binds S1P with high specificity and affinity; agonism of this receptor by the immunosuppressive agent FTY720 inhibits the entry of tissue T cells into afferent lymphatics in homeostatic and inflammatory conditions. Recent experiments have indicated that CCR7-deficient T cells left lymph nodes more rapidly than wild-type cells did and these cells where also less effectively retained after treatment with FTY720, and that egress competence could be restored by inactivating G alpha i-protein-coupled receptor signaling. These results suggest that S1P1 acts in the lymphocyte to promote lymph node egress by overcoming retention signals mediated by CCR7 and G alpha i-protein-coupled receptor signaling.

Supplier: Rockland Immunochemical

West Nile Virus (WNV) is a member of the Flaviviridae, a plus-stranded virus family that includes St. Louis encephalitis virus, yellow fever virus, and Dengue virus. WNV was initially isolated in 1937 in the West Nile region of Uganda and has become prevalent in Africa, Asia, and Europe. It has rapidly spread across the United States with cases being observed in every continental state. Virus particles consist of a dense core made up of the core/capsid protein encapsulating the RNA genome surrounded by a membrane envelope embedded with envelope and matrix proteins. However, when the viruses are inside of infected cells, the matrix protein exists in its "pre-M" form as a heterodimer with the envelope proteins. Cleavage of the "pre-M" protein to its mature form occurs during release of the virus; this cleavage leas to the dissociation of the heterodimers. The WNV receptor has recently been identified as alpha v beta 3 integrin.

Supplier: Prosci

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system, causing a hyperpolarization of the membrane through the opening of a Cl- channel associated with the GABAA-Receptor (GABAA-R) subtype. GABAA-Rs are important therapeutic targets for a range of sedative, anxiolytic, and hypnotic agents and are implicated in several diseases including epilepsy, anxiety, depression, and substance abuse. The GABAA-R is a multimeric subunit complex. To date six alphas, four betas and four gammas, plus alternative splicing variants of some of these subunits, have been identified. Injection in oocytes or mammalian cell lines of cRNA coding for alpha and beta subunits results in the expression of functional GABAA-Rs sensitive to GABA. However, coexpression of a gamma subunit is required for benzodiazepine modulation. The various effects of the benzodiazepines in brain may also be mediated via different alpha subunits of the receptor. Lastly, phosphorylation of beta subunits of the receptor has been shown to modulate GABAA-R function.

Supplier: Biosensis

Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, epinephrine and norepinephrine. Therefore the regulation of the TH enzyme represents the central means for controlling the synthesis of these important catecholamines. FUNCTION: Plays an important role in the physiology of adrenergic neurons. CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. COFACTOR: Fe(2+) ion. ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity. PATHWAY: Catecholamine biosynthesis; first step. SUBUNIT: Homotetramer. PTM: In vitro, phosphorylation of Ser-19 increases the rate of Ser-40 phosphorylation, which results in enzyme opening and activation. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. The presence of different DNA sequences at the TH locus confers susceptibility to various disorders of the brain including manic-depression and schizophrenia. Parkinson's disease is also considered a TH deficiency as low dopamine levels are a consistent neurochemical abnormality.