Masterflex+Single-use
Numéro de catalogue:
(BOSSBS-13110R-A488)
Fournisseur:
Bioss
Description:
Electron-transferring-flavoprotein dehydrogenase in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The protein is synthesized as a 67-kDa precursor which is targeted to mitochondria and processed in a single step to a 64-kDa mature form located in the mitochondrial membrane. Deficiency in electron-transferring-flavoprotein dehydrogenase have been demonstrated in some patients with type II glutaricacidemia. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 185 kDa, which is identified as c-erbB-2/HER-2/neu. Its epitope is localized in the extracellular domain. C-erbB-2/HER-2 is a member of the EGFR family. This MAb is specific and shows minimal cross-reaction with other members of the EGFR-family. Receptors of this family are located on the plasma membrane and consist of an extracellular ligand-binding domain that is connected to a large intracellular domain by a single transmembrane sequence. c-erbB-2/HER-2 protein is over-expressed in a variety of carcinomas especially those of breast and ovary.
Numéro de catalogue:
(BOSSBS-6765R-CY5.5)
Fournisseur:
Bioss
Description:
Perilipin is an intracellular neutral lipid droplet protein that is hormonally regulated. This protein is localized exclusively to the surface of lipid droplets. In response to lypotic stimuli, perilipin is phosphorylated by protein kinase A. Once activated, perilipin has inhibitory affects upon hormone-sensitive lipase (HSL), a protein that mediates the hydrolysis of triacylglycerol, the major form of stored energy in the body. Perilipin expression is limited to adipocytes and steroidogenic cells. There are currently two known isoforms, Perilipin A and B. Both of these proteins are encoded by a single-copy gene and are the result of differential splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6765R-CY3)
Fournisseur:
Bioss
Description:
Perilipin is an intracellular neutral lipid droplet protein that is hormonally regulated. This protein is localized exclusively to the surface of lipid droplets. In response to lypotic stimuli, perilipin is phosphorylated by protein kinase A. Once activated, perilipin has inhibitory affects upon hormone-sensitive lipase (HSL), a protein that mediates the hydrolysis of triacylglycerol, the major form of stored energy in the body. Perilipin expression is limited to adipocytes and steroidogenic cells. There are currently two known isoforms, Perilipin A and B. Both of these proteins are encoded by a single-copy gene and are the result of differential splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11070R-HRP)
Fournisseur:
Bioss
Description:
The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO-1, AMIGO-2 and AMIGO-3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO-1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO-2 (Alivin-1) is crucial for depolarization-dependent survival. Similar to AMIGO-1 and AMIGO-2, AMIGO-3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9500R-FITC)
Fournisseur:
Bioss
Description:
Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9501R-CY3)
Fournisseur:
Bioss
Description:
Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (Prothrombin and Factors X, IX, V and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble Fibrin clots and the promotion of platelet aggregation. Coagulation Factor X (Stuart Prower factor, FX, F10) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor. The mature form of Factor X (Factor X A) is generated by Factor IX A- or Factor VII A-mediated cleavage at the tripeptide sequence, Arg-Lys-Arg, to yield a disulfide linked dimer. Together with the cofactor Factor V A and Ca2+ on the surface of platelets or endothelial cells, Factor X A coordinates as part of the prothrombinase complex, which mediates proteolysis of Prothrombin into active Thrombin. Mutations at the Factor X locus resulting in Factor X deficiencies can contribute to hemorrhagic diathesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13621R-A680)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-9A (C-type lectin domain family 9 member A), also known as DNGR1 (dendritic cell natural killer lectin group receptor 1), is a 241 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Expressed in myeloid lineage cells, brain, spleen and thymus, CLEC-9A is a group V C-type lectin-like receptor (CTLR) that acts as an activation receptor. The gene encoding CLEC-9A maps to human chromosome 12p13.2 and mouse chromosome 6 F3.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13620R-HRP)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-9A (C-type lectin domain family 9 member A), also known as DNGR1 (dendritic cell natural killer lectin group receptor 1), is a 241 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Expressed in myeloid lineage cells, brain, spleen and thymus, CLEC-9A is a group V C-type lectin-like receptor (CTLR) that acts as an activation receptor. The gene encoding CLEC-9A maps to human chromosome 12p13.2 and mouse chromosome 6 F3.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13620R-A750)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-9A (C-type lectin domain family 9 member A), also known as DNGR1 (dendritic cell natural killer lectin group receptor 1), is a 241 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Expressed in myeloid lineage cells, brain, spleen and thymus, CLEC-9A is a group V C-type lectin-like receptor (CTLR) that acts as an activation receptor. The gene encoding CLEC-9A maps to human chromosome 12p13.2 and mouse chromosome 6 F3.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13620R-A350)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-9A (C-type lectin domain family 9 member A), also known as DNGR1 (dendritic cell natural killer lectin group receptor 1), is a 241 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Expressed in myeloid lineage cells, brain, spleen and thymus, CLEC-9A is a group V C-type lectin-like receptor (CTLR) that acts as an activation receptor. The gene encoding CLEC-9A maps to human chromosome 12p13.2 and mouse chromosome 6 F3.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11960R-A647)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK6 (SLIT and NTRK-like family, member 6) is an 841 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in select brain tissue, as well as in both adult and fetal lung, SLITRK6 functions to suppress neurite outgrowth, playing a role in the regulation of neuronal function. Multiple isoforms of SLITRK6 exist due to alternative splicing events.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.
Fournisseur:
Biotium
Description:
This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.
Fournisseur:
Biotium
Description:
This MAb recognizes an epitope within the 74-182 C-terminal sequence (11kD peptide fragment) of human serum Cellular Retinol Binding Protein 1 (CRBP 1), a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for transport of retinol (vitamin A1) from the liver to peripheral target tissues, like the eye, where it mediates the cellular uptake. CRBP 1 is synthesized by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex, which is big enough not to be lost by filtration through the kidney glomeruli. It is detected in nearly all tissues with higher expression in adult ovary, pancreas, pituitary gland, adrenal gland, and fetal liver.
Numéro de catalogue:
(BOSSBS-12141R-CY3)
Fournisseur:
Bioss
Description:
LRFN1 is a 771 amino acid single-pass type I membrane protein that belongs to the LRFN family. Containing a fibronectin type-III domain, an Ig-like (immunoglobulin-like) domain, a LRRCT domain, a LRRNT domain and seven LRR (leucine-rich) repeats, LRFN1 is thought to promote neurite outgrowth in hippocampal neurons and is involved in the regulation and maintenance of excitatory synapses. LRFN1 forms heteromeric complexes with LRFN2, LRFN3, LFRN4 and LFRN5, but does not have the ability to form homomeric complexes across cell junctions of adjacent cells like other LRFN family members. The PDZ-binding motif of LRFN1 is required for neurite outgrowth promotion and for SAP 97-, NE-dlg- and PSD-95-binding. LRFN1 is encoded by a gene located on human chromosome 19q13.2 and mouse chromosome 7 A3.
UOM:
1 * 100 µl
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