You Searched For: Quinoxaline-2,3-diamine

Catalog Number: (BTIUBNUM0419-50)

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

UOM: 1 * 50 µl

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Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Supplier: Biotium

Description: This monoclonal antibody is part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. This MAb recognizes the double stranded DNA in human cells. It can be used to stain the nuclei in cell or tissue preparations and can be used as a nuclear marker in human cells. This MAb produces a homogeneous staining pattern in the nucleus of normal and malignant cells.,Double Stranded deoxyribonucleic acid (ds DNA) is the genetic material of all cells and many viruses and is a polymer of nucleotides. The monomer consists of phosphorylated 2-deoxyribose N-glycosidically linked to one of four bases, adenine, cytosine, guanine or thymine. These are linked together by 3',5'-phosphodiester bridges. In the Watson-Crick double-helix model, two complementary strands are wound in a right-handed helix and held together by hydrogen bonds between complementary base pairs.

Catalog Number: (PRSI33-469)

Supplier: ProSci Inc.

Description: This mAb recognises TGF beta 1, 2 and 3. Three TGFbs have been identified in mammals. TGFb1, TGFb2 and TGFb3 are each synthesised as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGFb requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGFb3 protein has approximately 80% identity to the mature region of both TGFb1 and TGFb2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGFb's inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

UOM: 1 * 100 µG

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Catalog Number: (PRSI79-567)

Supplier: ProSci Inc.

Description: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.

UOM: 1 * 100 µG

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Catalog Number: (PRSI79-586)

Supplier: ProSci Inc.

Description: PDGF Receptor beta encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. This gene is flanked on chromosome 5 by the genes for granulocyte-macrophage colony-stimulating factor and macrophage-colony stimulating factor receptor; all three genes may be implicated in the 5-q syndrome. A translocation between chromosomes 5 and 12, that fuses this gene to that of the translocation, ETV6, leukemia gene, results in chronic myeloproliferative disorder with eosinophilia.

UOM: 1 * 100 µG

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Catalog Number: (PRSI79-178)

Supplier: ProSci Inc.

Description: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.

UOM: 1 * 100 µG

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Catalog Number: (BOSSBS-15573R-CY3)

Supplier: Bioss

Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-15573R-A350)

Supplier: Bioss

Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-15573R-FITC)

Supplier: Bioss

Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-15573R-A680)

Supplier: Bioss

Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13447R-CY3)

Supplier: Bioss

Description: Glycogen synthesis is initiated by the autoglucosylation of Glycogenin-1. Specifically, Glycogenin-1 glucosylates itself to begin the synthesis of glycogen in mammalian skeletal muscle. It acts as the primer to which further glucose monomers may be added. All of the Glycogenin-1 molecules contain at least one glucosyl residue before autoglucosylation begins. The first step of the glycogen synthesis occurs when a glucose molecule from UDP-glucose binds to the hydroxyl group of Tyr 194 on the Glycogenin-1 molecule. Using its glucosyltransferase activity, Glycogenin-1 adds more glucoses, each one coming from UDP-glucose. The glycosylation process reaches a plateau when five new glucose residues have been added, at which point glycogen synthase (GS) takes over and further elongates the chain. Glycogenin-1 remains covalently attached to the reducing end of the glycogen molecule.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13447R-A647)

Supplier: Bioss

Description: Glycogen synthesis is initiated by the autoglucosylation of Glycogenin-1. Specifically, Glycogenin-1 glucosylates itself to begin the synthesis of glycogen in mammalian skeletal muscle. It acts as the primer to which further glucose monomers may be added. All of the Glycogenin-1 molecules contain at least one glucosyl residue before autoglucosylation begins. The first step of the glycogen synthesis occurs when a glucose molecule from UDP-glucose binds to the hydroxyl group of Tyr 194 on the Glycogenin-1 molecule. Using its glucosyltransferase activity, Glycogenin-1 adds more glucoses, each one coming from UDP-glucose. The glycosylation process reaches a plateau when five new glucose residues have been added, at which point glycogen synthase (GS) takes over and further elongates the chain. Glycogenin-1 remains covalently attached to the reducing end of the glycogen molecule.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13447R-HRP)

Supplier: Bioss

Description: Glycogen synthesis is initiated by the autoglucosylation of Glycogenin-1. Specifically, Glycogenin-1 glucosylates itself to begin the synthesis of glycogen in mammalian skeletal muscle. It acts as the primer to which further glucose monomers may be added. All of the Glycogenin-1 molecules contain at least one glucosyl residue before autoglucosylation begins. The first step of the glycogen synthesis occurs when a glucose molecule from UDP-glucose binds to the hydroxyl group of Tyr 194 on the Glycogenin-1 molecule. Using its glucosyltransferase activity, Glycogenin-1 adds more glucoses, each one coming from UDP-glucose. The glycosylation process reaches a plateau when five new glucose residues have been added, at which point glycogen synthase (GS) takes over and further elongates the chain. Glycogenin-1 remains covalently attached to the reducing end of the glycogen molecule.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10493R-A680)

Supplier: Bioss

Description: Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesised as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesised as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesised as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10493R-A750)

Supplier: Bioss

Description: Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesised as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesised as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesised as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.

UOM: 1 * 100 µl

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