373661 Results for: "single-use assemblies"

Supplier: Genetex

Syntaxin 1, also known as HPC1, is a 35 kDa integral membrane protein which along with SNAP25, and VAMP/synaptobrevin plays a role in vesicular trafficking and membrane fusion. Two Syntaxin 1 isoforms have been identified, Syntaxin 1A which is localized to nerve terminals of sensory neurons and nerve fibers reaching small blood vessels, and Syntaxin 1B which is localized to motor end plates and muscle spindles. The SNARE (soluble N-ethylmaleimide sensitive fusion protein [NSF] attachment protein [SNAPs] receptors)hypothesis of membrane fusion proposes that Syntaxin 1A and SNAP25 (target membrane SNAREs, t-SNAREs) and VAMP/synaptobrevin (vesicular SNAREs, vSNAREs) bind together to form a tripartite structure that along with soluble cytosolic proteins allows for close membrane apposition of donor and target membranes thereby facilitating membrane fusion. The interaction of Syntaxin 1A with vSNAREs is thought to be negatively regulated by the binding of Munc18 to Syntaxin 1A and this interaction is controlled by Cdk5 phosphorylation of Munc18. Syntaxin 1A can be phosphorylated by casein kinase II and phosphorylation of Syntaxin enhances its interaction with Synaptotagmin.

Supplier: BioVendor

Zymogen granule membrane protein 16 (ZG16) is a 16 kDa protein first identified by immunoscreening of a rat pancreatic cDNA expression library with a polyspecific antiserum raised against purified zymogen granule membranes (ZGM). ZG16 displays sequence homology especially in the carbohydrate recognition domain to the plant lectin jacalin, which recognizes terminal galactose attached to N-acetylgalactosamine by a β1–3 linkage. According to its sequence homology with this lectin, ZG16 was considered a secretory lectin ZG16. Sequence analyses uncovered that ZG16 is highly conserved amongst mammals but also appears in many other species. Rat ZG16 was found to be highly expressed in pancreas, colon, and duodenum, where the protein was localized in the zymogen granule of pancreas. The previous reports indicated that rat ZG16 took part in the formation of zymogen granule by mediating the digested enzymes to the zymogen granule membrane in pancreatic acinar cells. Human ZG16 was shown to be highly expressed in adult liver and moderately expressed in intestine (jejunum, ileum) and colon. Moreover, ZG16 is also weakly expressed in pedunculus cerebellaris but not in other brain’s regions. Owing to the specific expression pattern in human liver, ZG16 was evaluated in hepatocellular carcinoma (HCC), a common cancer worldwide (it was found that human ZG16 was significantly down-regulated in HCC). ZG16 protein took part also in several secretions of glycoproteins (the secretion of human ZG16 would be affected when the synthesis of glycans was inhibited with inhibitor or without glucose in cell culture).

Supplier: Biosensis

BDNF belongs to the neurotrophin family and promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. It is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family.

Supplier: Prosci

Interleukin-23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12 (1-5). Although p19 is expressed by activated macrophages, dendritic cells, T cells, and endothelial cells, only activated macrophages and dendritic cells express p40 concurrently to produce IL-23. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 Rbeta1) and the IL-23-specific receptor subunit (IL-23 R). IL-23 has biological activities that are similar to, but distinct from IL-12. Both IL-12 and IL-23 induce proliferation and IFN-gamma production by human T cells. While IL-12 acts on both naie and memory human T cells, the effects of IL-23 is restricted to memory T cells. In mouse, IL-23 but not IL-12, has also been shown to induce memory T cells to secret IL-17, a potent proinflammatory cytokine. IL-12 and IL-23 can induce IL-12 production from mouse splenic DC of both the CD8-and CD8+ subtypes, however only IL-23 can act directly on CD8+ DC to mediate immunogenic presentation of poorly immunogenic tumor/self peptide.

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) DyLight™ 800 Conjugated antibody generated in rabbit detects specifically monkey IgG heavy and light chains. 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. Both heavy and light chains of the antibody molecule are present. This DyLight™800 conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform immunofluorescence, flow cytometry, 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.The emission spectra for this DyLight™ conjugate match the principle output wavelengths of most common fluorescence instrumentation.

Supplier: Prosci

It recognizes a polypeptide of 6.5kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Rockland Immunochemical

Anti-Monkey IgG (gamma chain) DyLight™680 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™680 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: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is significant for researchers involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic and cardiovascular diseases.

Supplier: Rockland Immunochemical

NLRP3(NLR FAMILY, PYRIN DOMAIN-CONTAINING 3),also known as CIAS1, CRYOPYRIN, NALP3 or PYPAF1, is a protein that in humans is encoded by the NLRP3 (NOD-like receptor family, pryin domain containing 3) gene. The NLRP3 gene encodes a pyrin-like protein expressed predominantly in peripheral blood leukocytes. And the NLRP3 gene is mapped on 1q44. NLRP3 interacts with apoptosis-associated speck-like protein containing a CARD (ASC). The encoded protein may play a role in the regulation of inflammation and apoptosis. Mutation of the NALP3 nucleotide-binding domain reduced ATP binding, CASP1 activation, IL1B production, cell death, macromolecular complex formation, self-association, and association with ASC. Consistent with an essential role for Nlrp3 inflammasomes in antifungal immunity, Gross et al.showed that Nlrp3-deficient mice are hypersusceptible to C. albicans infection. Activation of the NLRP3 inflammasome in response to virus or to RNA was dependent upon lysosomal maturation and reactive oxygen species production in human cells. The NLRP3 inflammasome senses obesity-associated danger signals and contributes to obesity-induced inflammation and insulin resistance. This antibody is suitable for researchers interested in cancer research.

Supplier: 3M Healthcare

3M™ 3MDW301 Under Sink Dedicated Faucet Water Filter System – premium performance for home water purification. This system is NSF listed for quality assurance and will reduce particulate, chlorine taste & odor, chloramine, asbestos, parasitic protozoan cysts, lead, MTBE, trihalomethanes (TTHM), VOCs and comes with a dedicated drinking water system faucet that adds function and beauty.

Supplier: SenseAnywhere

Explore the SenseAnywhere StarterKit −200 to +200 °C for unparalleled temperature surveillance in extreme environments. Integrating the AiroSensor 20-20-43 and a PT100 Probe, it offers accurate readings for cryogenic applications. Simplified calibration, robust Indoor AccessPoint, and innovative AssetTagging ensure continuous, secure data transmission and seamless sensor management in demanding conditions.

Supplier: Prosci

Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-κ-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652', leading to activate the NF-κ-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters.

Supplier: Rockland Immunochemical

Conjugated Anti-Monkey IgG (H&L) DyLight™ 680 Conjugated antibody generated in rabbit detects specifically monkey IgG heavy and light chains. 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. Both heavy and light chains of the antibody molecule are present. This DyLight™680 conjugated anti-Monkey IgG (H&L) secondary antibody is ideal for investigators who routinely perform immunofluorescence, flow cytometry, 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. The emission spectra for this DyLight™ conjugate match the principle output wavelengths of most common fluorescence instrumentation.

Supplier: IBI Scientific

Select-D Columns are ideal for desalting and removing unincorporated radiolabeled deoxynucleotide triphosphates from end labels, fill in, nick-translation, or random primed DNA labeling reactions

Supplier: Cell Biolabs

QuickTiter™ Lentivirus Quantitation Kit provides a quick method for measuring the viral nucleic acid content of your lentivirus prep

Supplier: Prosci

Recognizes a protein of 47-55kDa, which is identified as FOXP3. Its precise epitope is not known, but it has been mapped to the N-terminal portion of the protein. The FOX family of transcription factors is a large group of proteins that share a common DNA binding domain termed a winged-helix or forkhead domain. During early development, FOXP1 and FOXP2 are expressed abundantly in the lung, with lower levels of expression in neural, intestinal and cardiovascular tissues, where they act as transcription repressors. FOXP1 is widely expressed in adult tissues, while neoplastic cells often exhibit a dramatic change in expression level or localization of FOXP1. Mutations in FOXP3 gene cause IPEX, a fatal, X-linked inherited disorder characterized by immune dysregulation. The FOXP3 protein is essential for normal immune homeostasis. Specifically, FOXP3 represses transcription through a DNA binding forkhead domain, thereby regulating T cell activation.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. /IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

Supplier: Zymo Research

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

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: Enzo Life Sciences

Rapid and complete removal of gDNA from RNA preps.

Supplier: IBI Scientific

Supplemental kit for IBI Tri-Isolate RNA Pure Kit when working with bacterial cells.

Supplier: BioVendor

Cyclophilins belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity; such proteins are collectively known as immunophilins and also include the FK-506-binding proteins and the parvulins. Cyclophilins are found in all cells of all organisms studied, in both prokaryotes and eukaryotes. Human have a total of 16 cyclophilin proteins. Cyclophilins also have varying degrees of affinity for the immunosuppressive drug Cyclosporine A (CsA), a cyclic 11-amino-acid peptide produced by fungus Tolypocladium infantum. Cyclophilin A, in particular, is the major intracellular receptor for CsA. Cyclophilin A (CYPA) is the first member of the cyclophilins to be identified in mammals. Human genes of CYPA, also known as Cyp18, are located on chromosome 7p11.2-p13 and encode the protein, which consists of 165 amino acid residues with a relative molecular mass approximately 18 kDa. Human CYPA has an eight-stranded antiparallel β-barrel structure, with two α-helices enclosing the barrel from either side. Seven aromatic and other hydrophobic residues form a compact hydrophobic core within the barrel, usually in the area where CsA binds. A loop from Lys118 ti His126 and four β-strands (β3-β6) make up the binding site for CsA. In mammals, the CsA-CYPA complex binds to and inhibits calcineurin, a calcium-calmodulin-activated serine/threonine-specific protein phosphatase. The inhibition of calcineurin blocks the translocation of nuclear factor of activated T cells from the cytosol to the nucleus, thus preventing the transcription of genes encoding cytokines such as interleukin-2.

Supplier: New England Biolabs (NEB)

The Monarch spin columns S2A and tubes are a component of Monarch kits for RNA cleanup, and also offered separately for convenience and flexibility.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Rockland Immunochemical

Anti-Cyclin D3 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Cyclin D3 belongs to a highly conserved cyclin family, whose members are the ultimate recipients of oncogenic signals. Cyclin D3 is a key component of the cell cycle progression machinery and induces progression through the G1 phase of the cell cycle. Cyclin D3 is expressed in nearly all proliferating cells, and shows the most broad expression pattern of all three D-type (D1-D3) cyclins. Cyclin D3 is encoded from the 6p21 chromosome region and the protein is predominantly localized in the nucleus. Once induced, cyclin D3 binds and activates its associated cyclin-dependent kinases CDK4 and CDK6. Amplification of the cyclin D3 gene and overexpression of cyclin D3 protein is seen in several human cancers. A large number of human malignancies contain lesions in pathways impacting on cyclin D3. Abnormal expression of Cyclin D3 is believed to be a driving force in several human cancers. A possible role for cyclin D3 in the malignancies of the lymphoid system is suggested by the observations that cyclin D3 gene is rearranged in several neoplastic diseases such as diffuse large B cell lymphomas or multiple myelomas. Anti-Cyclin D3 is ideal for researchers interested in Cancer Research and Immunology research.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Omega Bio-Tek

The Mag-Bind® Blood DNA HDQ 96 Kit is designed for rapid and reliable isolation of high-quality genomic DNA from 100-200 μL blood samples

Supplier: Biosensis

GDNF is a glycosylated, disulfide-bonded homodimer molecule. It was first discovered as a potent survival factor for midbrain dopaminergic neurons and was then shown to rescue these neurons in animal models of Parkinson's disease. GDNF is about 100 times more efficient survival factor for spinal motor neurons than the neurotrophins. FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. DISEASE: Defects in GDNF may be a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, defects in GDNF may be involved in Hirschsprung disease. This genetic disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. DISEASE: Defects in GDNF are a cause of congenital central hypoventilation syndrome (CCHS); also known as congenital failure of autonomic control or Ondine curse. CCHS is a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.