776 Results for: "young+scientists+club"

Supplier: Southern Biotechnology

In the chicken, the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. Chicken CD8 is expressed on approximately 80% of thymocytes, 15% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. The monoclonal antibody CT-8 recognizes the CD8α chain and has been shown to react to a polymorphic determinant in turkey.

Supplier: Southern Biotechnology

In the chicken the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. Chicken CD8 is expressed on approximately 80% of thymocytes, 45% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. The monoclonal antibody 3-298 recognizes the CD8α chain of both the chicken and turkey.

Supplier: Southern Biotechnology

In the chicken the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. Chicken CD8 is expressed on approximately 80% of thymocytes, 45% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. The monoclonal antibody 3-298 recognizes the CD8α chain of both the chicken and turkey.

Supplier: Southern Biotechnology

In the chicken the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. Chicken CD8 is expressed on approximately 80% of thymocytes, 45% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. The monoclonal antibody 3-298 recognizes the CD8α chain of both the chicken and turkey.

Supplier: Southern Biotechnology

In the chicken, the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. Chicken CD8 is expressed on approximately 80% of thymocytes, 15% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. The monoclonal antibody CT-8 recognizes the CD8α chain and has been shown to react to a polymorphic determinant in turkey.

Supplier: Rockland Immunochemical

Anti-CD31 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). CD31 (PECAM-1) is a 130 kDa platelet endothelial cell adhesion molecule encoded by the PECAM1 gene found on chromosome 17 in humans. CD31 is expressed on platelets, monocytes, neutrophils, and some types of T-cells, and makes up a large portion of endothelial cell intercellular junctions. CD31 plays a key role in modulation of integrin-mediated cell adhesion, leukocyte transendothelial migration, angiogenesis, apoptosis and macrophage phagocytosis. CD31 is also expressed in certain tumors, including epithelioid hemangioendothelioma, epithelioid sarcoma-like hemangioendothelioma, other vascular tumors, histiocytic malignancies, and plasmacytomas. Anti-CD31 is ideal for researchers interested in Stem Cell Research, Epigenetics, and Cell-cycle Regulation research.

Supplier: Southern Biotechnology

In the chicken, the CD8 molecule is present in two forms - (i) a homodimer of two α chains and (ii) a heterodimer of an α chain and a β chain. While the vast majority of CD8+ cells in the thymus, spleen, and blood of adult chickens express both CD8α- and CD8β-chains, a relatively large proportion of the CD8+ TCRγδ cells in the spleens of embryos and young chicks express only the α-chain of CD8. Among intestinal epithelial lymphocytes, the major CD8+ T cell populations present in mice are conserved but there is a population of TCRγδ CD8αβ cells in the chicken that is not found in rodents. Chicken CD8 is expressed on approximately 80% of thymocytes, 15% of blood mononuclear cells, and 50% of spleen cells but less than 1% of cells in the bursa and bone marrow. The monoclonal antibody CT-8 recognizes the CD8α chain and has been shown to react to a polymorphic determinant in turkey.

Supplier: Rockland Immunochemical

Anti-NEMO antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Anti-NEMO antibody detects recombinant and endogenous NEMO. NEMO, the regulatory subunit of the IKK core complex, phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Nemo is also considered to be a mediator for TAX activation of NF-kappa-B and may be implicated in NF-kappa-B-mediated protection from cytokine toxicity. NEMO is essential for viral activation of IRF3 and involved in TLR3- and IFIH1-mediated antiviral innate response. The innate antivaral response from NEMO requires 'Lys-27'-linked polyubiquitination. Anti-NEMO is ideal for researchers interested in Immunology and Cancer research.

Supplier: Spectrum Chemical Mfg. Corp.

XYLITOL, NF is a naturally occurring 5-carbon sugar alcohol found in many fruits and vegetables. Xylitol is used as nutritive sweetener as a sugar substitute to produce “sugar-free” foods and is commonly used in the production of chewing gums, mints and other candies. It is healthier than sugar (75% fewer carbohydrates and 40% fewer calories) and just as sweet. Is often used in tooth care products and has proven to be healthier for teeth than sugar. Although its main use is as a food additive, it is also used medicinally to prevent middle ear infections in young children. The NF grade indicates it is graded suitable for personal care, cosmetic and pharmaceutical applications. All Spectrum Chemical NF grade products are manufactured, packaged and stored under current Good Manufacturing Practices (cGMP) per 21CFR part 211 in FDA registered and inspected facilities.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Rockland Immunochemical

Anti-NEMO antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Anti-NEMO antibody detects recombinant and endogenous NEMO. NEMO, the regulatory subunit of the IKK core complex, phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Nemo is also considered to be a mediator for TAX activation of NF-kappa-B and may be implicated in NF-kappa-B-mediated protection from cytokine toxicity. NEMO is essential for viral activation of IRF3 and involved in TLR3- and IFIH1-mediated antiviral innate response. The innate antivaral response from NEMO requires 'Lys-27'-linked polyubiquitination. Anti-NEMO is ideal for researchers interested in Immunology and Cancer research.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Bioss

Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.

Supplier: Stemcell Technologies

Stimulating T cells with EBV (EBNA-3A) Peptide Pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (EBNA-3A) Peptide Pool is a lyophilized mixture of 234 peptides from Epstein-Barr nuclear antigen 3 (EBNA-3A) of Epstein-Barr virus (EBV; strain B95-8) and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 - 944 on EBNA-3A. EBNA-3A contributes to B cell growth transformation (Hertle et al.; Tomkinson et al.) and has been found to interact with host cell proteins, where it activates (Young et al.) or represses (Cludts and Farrell; Hickabottom et al.) transcription of specific cellular genes. Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: Proteintech

NeuroD is a member of the basic helix-loop-helix (bHLH) family of transcription factors. The basic helix-loop-helix (bHLH) proteins are transcription factors that are required for several aspects of development, including cell type determination, terminal differentiation and sex determination. Members of the myogenic determination family, MyoD, myf5, myogenin and MRF4, all have bHLH domains.These proteins function by forming heterodimers with E-proteins and binding to the canonical E-box sequence CANNTG. Neuro D is expressed transiently in a subset of neurons in the central and peripheral nervous systems at the time of their terminal differentiation into mature neurons. Moreover, ectopic expression of Neuro D in Xenopus embryos induces premature differentiation of neuronal precursors and Neuro D can convert presumptive epidermal cells into neurons.The lack of NeuroD in the brain results in severe defects in development. Human mutations have been linked to a number of types of diabetes including type I diabetes mellitus and maturity-onset diabetes of the young.

Supplier: Boster Biological Technology

Polyclonal antibody for LAMIN A/LMNA detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. LAMIN A/LMNA information: Molecular Weight: 74139 MW; Subcellular Localization: Nucleus. Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin- A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C; Tissue Specificity: In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress.

Supplier: Rockland Immunochemical

Anti-Ezh1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Anti-EZH1 Antibody detects human EZH1. Polycomb group (PcG) proteins are essential epigenetic regulators in normal tissue homeostasis and are involved in transcriptional repression. The PcG members Ezh2 and Ezh1 are important determinants of embryonic stem cell identity, and the transcript levels of these histone methyltransferases are inversely correlated during development. Recent studies have shown that EZH1 also has histone H3K27 methyltransferase activity and binds to an overlapping subset of genes. EZH1 and EZH2 have different expression patterns. EZH2 is found in actively proliferating cells, whereas EZH1 expression is higher in nonproliferative adult tissues. EZH1 partially compensates for the loss of EZH2, as shown in cells lacking only Ezh2. In mice, EZH1 is a regulator of homeotic gene expression implicated in the assembly of repressive protein complexes in chromatin. Anti-EZH1 Antibody is ideal for investigators studying pathogenesis of hematological malignancies.

Supplier: Chem-Impex International

Supplier: Chem-Impex International

Supplier: Rockland Immunochemical

Anti-HSF1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Heat shock factor 1 (HSF1) is a highly conserved transcription factor that coordinates stress-induced transcription and directs versatile physiological processes in eukaryotes. Upon stress, HSF1 is the key transcriptional activator of chaperones, co-chaperones and ubiquitin, and also coordinates the expression of many transcriptional and translational regulators, signaling molecules and mitotic determinants. HSF1 is involved in balancing core cellular processes during stress and enables their rapid re-establishment once conditions suitable for proliferation have been restored. Importantly, HSF1 controls a distinct set of target genes in cell stress, development and cancer progression. The central role of HSF1 in diverse cellular functions is reflected in pathologies, such as neurodegenerative diseases and cancer, where an imbalance in HSF1 activity facilitates disease onset. The ability of cancer cells to harness HSF1 for metastatic progression highlights the plasticity of HSF1 in rewiring transcription and coordinating cellular processes. Anti-HSF1 antibody is thus ideal for investigators involved in cancer research and neurodegenerative diseases.

Supplier: Rockland Immunochemical

Anti-Ffar4 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Free Fatty Acid 4 receptor (Ffa4 receptor or GPR120), a rhodopsin-like G protein coupled receptor (GPCR) subfamily member, is a receptor that senses specific fatty acids such as omega-3 fatty acid in fish oil or the endogenous signaling lipid, PHASA. Ffa4 receptor is enriched in lung, colon and adipose tissue but is also detected in many other tissues and cells. The activation of Ffar4 has multiple effects, including but not limited to inhibition of inflammation, improving insulin sensitivity and adipogenesis, and regulating hormone secretion from the gastro-intestinal system and pancreatic islets. Therefore, approaches that regulate FFA4 receptor activity could be developed as promising anti-diabetic and anti-inflammation drugs. GPR120 is the only fatty acid receptor that can sense lipids in adipose tissue, mature adipocytes, CD11c+ macrophages, and RAW264.7 cells making this receptor of potential importance in the prevention and treatment of metabolic and inflammatory diseases.

Supplier: Rockland Immunochemical

Anti-Ffar4 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Free Fatty Acid 4 receptor (Ffa4 receptor or GPR120), a rhodopsin-like G protein coupled receptor (GPCR) subfamily member, is a receptor that senses specific fatty acids such as omega-3 fatty acid in fish oil or the endogenous signaling lipid, PHASA. Ffa4 receptor is enriched in lung, colon and adipose tissue but is also detected in many other tissues and cells. The activation of Ffar4 has multiple effects, including but not limited to inhibition of inflammation, improving insulin sensitivity and adipogenesis, and regulating hormone secretion from the gastro-intestinal system and pancreatic islets. Therefore, approaches that regulate FFA4 receptor activity could be developed as promising anti-diabetic and anti-inflammation drugs. GPR120 is the only fatty acid receptor that can sense lipids in adipose tissue, mature adipocytes, CD11c+ macrophages, and RAW264.7 cells making this receptor of potential importance in the prevention and treatment of metabolic and inflammatory diseases.

Supplier: Rockland Immunochemical

Anti-Ezh1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Anti-EZH1 Antibody detects human EZH1. Polycomb group (PcG) proteins are essential epigenetic regulators in normal tissue homeostasis and are involved in transcriptional repression. The PcG members Ezh2 and Ezh1 are important determinants of embryonic stem cell identity, and the transcript levels of these histone methyltransferases are inversely correlated during development. Recent studies have shown that EZH1 also has histone H3K27 methyltransferase activity and binds to an overlapping subset of genes. EZH1 and EZH2 have different expression patterns. EZH2 is found in actively proliferating cells, whereas EZH1 expression is higher in nonproliferative adult tissues. EZH1 partially compensates for the loss of EZH2, as shown in cells lacking only Ezh2. In mice, EZH1 is a regulator of homeotic gene expression implicated in the assembly of repressive protein complexes in chromatin. Anti-EZH1 Antibody is ideal for investigators studying pathogenesis of hematological malignancies.

Supplier: Rockland Immunochemical

Anti-HSF1 Antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Heat shock factor 1 (HSF1) is a highly conserved transcription factor that coordinates stress-induced transcription and directs versatile physiological processes in eukaryotes. Upon stress, HSF1 is the key transcriptional activator of chaperones, co-chaperones and ubiquitin, and also coordinates the expression of many transcriptional and translational regulators, signaling molecules and mitotic determinants. HSF1 is involved in balancing core cellular processes during stress and enables their rapid re-establishment once conditions suitable for proliferation have been restored. Importantly, HSF1 controls a distinct set of target genes in cell stress, development and cancer progression. The central role of HSF1 in diverse cellular functions is reflected in pathologies, such as neurodegenerative diseases and cancer, where an imbalance in HSF1 activity facilitates disease onset. The ability of cancer cells to harness HSF1 for metastatic progression highlights the plasticity of HSF1 in rewiring transcription and coordinating cellular processes. Anti-HSF1 antibody is thus ideal for investigators involved in cancer research and neurodegenerative diseases.

Supplier: Rockland Immunochemical

Anti-Nuclear receptor ROR gamma pS203 was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Nuclear receptor ROR gamma pS203 antibody detects mouse receptor ROR gamma phosphorylated at the serine 203 position. RAR-related orphan receptor gamma is a member of the nuclear receptor family of transcription factors. (ROR-gamma) is a key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. ROR-gamma regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. It is also involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism and is a negative regulator of adipocyte differentiation. It controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. Isoform 2, ROR-gamma is essential for lymphoid organogenesis, in particular lymph nodes and Peyer's patches. ROR-gamma also plays an important regulatory role in thymopoiesis, and in inhibiting apoptosis of undifferentiated T cells. Anti-nuclear receptor ROR gamma pS203 is ideal for researcher's interested in autoimmune diseases such as psoriasis and rheumatoid arthritis, circadian rhythms, and immune system disorders.

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

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.