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Catalog Number: (BOSSBS-1906R-CY3)
Supplier: Bioss
Description: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1906R-A555)
Supplier: Bioss
Description: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5915R)
Supplier: Bioss
Description: DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1906R-CY5)
Supplier: Bioss
Description: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1906R)
Supplier: Bioss
Description: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1906R-HRP)
Supplier: Bioss
Description: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
UOM: 1 * 100 µl


Catalog Number: (118-0253)
Supplier: ORKLA CARE
Description: This plastic, case with transparent lid and handle, contains five bottles of Cederroth eyewash solution. The solution is intended for washing away particles and dangerous liquids, like alkali or acids, from an eye in an emergency situation in the workplace.
UOM: 1 * 1 items


Supplier: MP Biomedicals
Description: Choline bitartrate is a acyl group acceptor. Bitarate is added to the choline to speed up the absorption rate within the human body. Choline Bitartrate is an essential nutrient, generally grouped as a B vitamin, that helps to improve cognitive function and aids fat metabolism.

Catalog Number: (BOSSBS-5952R-CY3)
Supplier: Bioss
Description: POMT1 (Protein O mannosyl transferase 1) is a multipass membrane protein that is found in the endoplasmic reticulum. POMT1 catalyses the transfer of mannosyl residues to the hydroxyl groups of serine or threonine residues. Enzymatic activity is dependent on co expression of POMT1 with POMT2. Defects in the POMT1 gene are associated with Walker-Warburg syndrome (WWS), a congential muscular dystrophy that is associated with mental retardation and is usually lethal within the first few months of life. Other defects in the POMT1 gene result in limb girdle muscular dystrophy type 2K (LGMD2K), which is associated with mild mental retardation. Studies in Drosophila suggest that mutation of POMT1 alters the efficacy of synaptic transmission and a change in subunit composition of post synaptic glutamate receptors at the neuromuscular junction. Missense mutations in POMT1 have been associated with glioneuronal and glial brain tumours.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5952R-HRP)
Supplier: Bioss
Description: POMT1 (Protein O mannosyl transferase 1) is a multipass membrane protein that is found in the endoplasmic reticulum. POMT1 catalyses the transfer of mannosyl residues to the hydroxyl groups of serine or threonine residues. Enzymatic activity is dependent on co expression of POMT1 with POMT2. Defects in the POMT1 gene are associated with Walker-Warburg syndrome (WWS), a congential muscular dystrophy that is associated with mental retardation and is usually lethal within the first few months of life. Other defects in the POMT1 gene result in limb girdle muscular dystrophy type 2K (LGMD2K), which is associated with mild mental retardation. Studies in Drosophila suggest that mutation of POMT1 alters the efficacy of synaptic transmission and a change in subunit composition of post synaptic glutamate receptors at the neuromuscular junction. Missense mutations in POMT1 have been associated with glioneuronal and glial brain tumours.
UOM: 1 * 100 µl


Catalog Number: (RETS02.486.0055)
Supplier: Retsch GmbH
Description: Opening aid for safety closure device
UOM: 1 * 1 items


Catalog Number: (BOSSBS-13447R-FITC)
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


Catalog Number: (BOSSBS-1437R-HRP)
Supplier: Bioss
Description: MRP5 (190-200 kDa) is closely related to MRP4, both lacking the first five membrane spanning regions. MRP5 is a GS-X multi specific organic anion pump (nucleotide analogs). MRP5 may transport DNP-GS and may be inhibited by certain inhibitors of organic anion transport (sulfinpyrazone). MRP5 may also transport organic anions with the anionic moiety of phosphate/phosphonate group, a function which provides the ability to resist against anti cancer drugs 6-MP and thioguanine as well as the anti-HIV drug PMEA.
UOM: 1 * 100 µl


Catalog Number: (BSENM-1702-100)
Supplier: Biosensis
Description: High-mobility group proteins were named originally since they are abundand relatively low molecular weight proteins which run quickly on SDS-PAGE gels. High-mobility group protein box 1 (HMGB1, Amphoterin) is one of these. The "bx" in the name refers to the so-called high mobility group (HMG) box, a compact domain involved in DNA binding and protein-protein interactions. the HMGB1 molecule has two of these HMG domains. The protein is alslo called amphoterin, this name being derived from the presence of two highly charged regions in the molecule, a relatively neutrally charged N-terminus and a very negatively charged C-terminus. In fact the molecule is very unusually charged throughout, the human sequence consisting of 16.7% Glutamic acid, 9.3% Aspartic acid, 20% lysine and 9.3% Arginine. HMGB1 can bind Toll like receptor 4 (TLR4) and the Receptor for Advanced Glycation End products (RAGE). TLRs are components of the innate immune system, first recognized as a family of receptors which recognize "Pathogen Associated Molecular Pattern molecules (PAMPs). PAMPs are common components of bacteria and when TLRs bind these a strong inflammatory response is activated. More recently it has been recognized that TLRs can also be activated by Damage Associated Molecular Pattern molecules (DAMPs), which are endogenous substances released from damaged and diseased cells which also bind to TLR family receptors and also activate inflammation. HMGB1 is such a DAMP, binding to TLR4, and much evidence suggests that HMGB1 is a strong activator of inflammation. Interestingly, HMGB1 is released by necrotic cells but not by apoptotic cells (1).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13447R-CY5)
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


Catalog Number: (BOSSBS-2190R-A647)
Supplier: Bioss
Description: Cytokeratins, a group comprising at least 29 different proteins, are characteristic of epithelial and trichocytic cells. Cytokeratins 1, 4, 5, 6, and 8 are members of the type II neutral to basic subfamily. Antibody to cytokeratins are specific markers of epithelial cell differentiation and have been widely used as tools in tumor identification and classification. Anti Pan Cytokeratin (mixture) is a broadly reactive reagent, which recognizes epitopes present in most human epithelial tissues. It facilitates typing of normal, metaplastic and neoplastic cells. Synergy between the various components results in staining amplification. This enables identification of cells, which would otherwise be stained only marginally. The mixture may aid in the discrimination of carcinomas and nonepithelial tumors such as sarcomas, lymphomas and neural tumors. It is also useful in detecting micrometastases in lymph nodes, bone marrow and other tissues and for determining the origin of poorly differentiated tumors. There are two types of cytokeratins the acidic type I cytokeratins and the basic or neutral type II cytokeratins. Cytokeratins are usually found in pairs comprising a type I cytokeratin and a type II cytokeratin. Usually the type II cytokeratins are 8kD larger than their type I counterparts.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at +43 1 97002 - 0.
Dual use goods can only be delivered within the European Union.
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