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Fournisseur:  Bioss
Description:   Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11183R-A350)

Fournisseur:  Bioss
Description:   Extracellular proteases mediate the digestion of neighboring extracellular matrix components in initial tumor growth, allow desquamation of tumor cells into the surrounding environment, provide the basis for invasion of basement membranes in targeted metastatic organs and are required for release and activation of many growth and angiogenic factors. TMPRSS5 (transmembrane protease, serine 5), also known as spinesin, is a 457 amino acid single-pass type II membrane protein that is expressed specifically in brain and is thought to play a role in hearing. A member of the peptidase S1 family, TMPRSS5 contains one peptidase S1 domain and an SRCR domain, and is encoded by a gene that maps to human chromosome 11q23.2. Defects in the gene encoding TMPRSS5 are associated with deafness.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-10465R-A555)

Fournisseur:  Bioss
Description:   Alpha-1-adrenergic receptors (alpha-1-ARs) are members of the G protein-coupled receptor superfamily. They activate mitogenic responses and regulate growth and proliferation of many cells. There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and different subtypes show different patterns of activation. This gene encodes alpha-1B-adrenergic receptor, which induces neoplastic transformation when transfected into NIH 3T3 fibroblasts and other cell lines. Thus, this normal cellular gene is identified as a protooncogene. This gene comprises 2 exons and a single large intron of at least 20 kb that interrupts the coding region. [provided by RefSeq, Jul 2008].
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11183R-A647)

Fournisseur:  Bioss
Description:   Extracellular proteases mediate the digestion of neighboring extracellular matrix components in initial tumor growth, allow desquamation of tumor cells into the surrounding environment, provide the basis for invasion of basement membranes in targeted metastatic organs and are required for release and activation of many growth and angiogenic factors. TMPRSS5 (transmembrane protease, serine 5), also known as spinesin, is a 457 amino acid single-pass type II membrane protein that is expressed specifically in brain and is thought to play a role in hearing. A member of the peptidase S1 family, TMPRSS5 contains one peptidase S1 domain and an SRCR domain, and is encoded by a gene that maps to human chromosome 11q23.2. Defects in the gene encoding TMPRSS5 are associated with deafness.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].
UOM:  1 * 100 µl
Numéro de catalogue: (ENZOADICSA330E)

Fournisseur:  ENZO LIFE SCIENCES
Description:   The epidermal growth factor receptor (EGFR) is a 170-kDa membrane bound receptor consisting of an extracellular ligand-binding domain, a single hydrophobic transmembrane region, and a tyrosine kinase domain-containing cytoplasmic region. Ligand binding induces receptor homo- or heterodimerization, triggering autophosphorylation of cytoplasmic tyrosine residues that provide docking sites for Src homology 2 (SH2) domain-containing signaling molecules. Src-mediated phosphorylation of EGFR at Tyr845 may contribute to EGFR hyperactivity in cancer, while autophosphorylation of EGFR at Tyr1068 and/or Tyr1173 in response to ligand binding is known to recruit cofactors (e.g. SHP1, RasGAP, SOS1, Grb2) that activate pathways associated with cell growth, apoptosis, adhesion, receptor endocytosis, and protein degradation.
UOM:  1 * 1 EA
New Product
Numéro de catalogue: (BOSSBS-11087R-CY5)

Fournisseur:  Bioss
Description:   LRFN2 is a 789 amino acid single-pass type I membrane protein belonging to the LRFN family. Encoded by a gene that maps to human chromosome 6p21.2, LRFN2 is moderately expressed in brain, spleen and testis. LRFN2 contains one fibronectin type-III domain, one Ig-like (immunoglobulin-like) domain and six LRR (leucine-rich) repeats. LRFN2 promotes neurite outgrowth in hippocampal neurons, enhances cell surface expression of two NMDA receptor subunits, NMDAΩ1 and NMDAé1, and may play a role in redistributing PSD-95 to cell periphery. LRFN2 forms heteromeric complexes with LRFN1, LRFN3, LRFN4 and LRFN5, and is capable of forming homomeric complexes, but not across cell junctions.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11863R-CY5)

Fournisseur:  Bioss
Description:   Shootin1 is a 631 amino acid protein that belongs to the shootin family. The shootin1 protein contains three coiled-coil domains, a proline-rich region and interacts with RUFY3. Shootin1 is involved in the generation of internal asymmetric signals required for neuronal polarization. The shootin1 protein acts upstream of PI3K (phosphoinositide 3-kinase), by being required for spatially localized PI3K activity. By accumulating asymmetrically in a single neurite before polarization, shootin1 leads to axon induction for polarization, additionally the absence of shootin1 from the nascent axon's siblings by competition prevents the formation of surplus axons. Existing as seven alternatively spliced isoforms, the shootin1 gene is conserved in chimpanzee, dog, mouse, rat, chicken and zebrafish, and maps to human chromosome 10q25.3.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11863R-CY7)

Fournisseur:  Bioss
Description:   Shootin1 is a 631 amino acid protein that belongs to the shootin family. The shootin1 protein contains three coiled-coil domains, a proline-rich region and interacts with RUFY3. Shootin1 is involved in the generation of internal asymmetric signals required for neuronal polarization. The shootin1 protein acts upstream of PI3K (phosphoinositide 3-kinase), by being required for spatially localized PI3K activity. By accumulating asymmetrically in a single neurite before polarization, shootin1 leads to axon induction for polarization, additionally the absence of shootin1 from the nascent axon's siblings by competition prevents the formation of surplus axons. Existing as seven alternatively spliced isoforms, the shootin1 gene is conserved in chimpanzee, dog, mouse, rat, chicken and zebrafish, and maps to human chromosome 10q25.3.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Shootin1 is a 631 amino acid protein that belongs to the shootin family. The shootin1 protein contains three coiled-coil domains, a proline-rich region and interacts with RUFY3. Shootin1 is involved in the generation of internal asymmetric signals required for neuronal polarization. The shootin1 protein acts upstream of PI3K (phosphoinositide 3-kinase), by being required for spatially localized PI3K activity. By accumulating asymmetrically in a single neurite before polarization, shootin1 leads to axon induction for polarization, additionally the absence of shootin1 from the nascent axon's siblings by competition prevents the formation of surplus axons. Existing as seven alternatively spliced isoforms, the shootin1 gene is conserved in chimpanzee, dog, mouse, rat, chicken and zebrafish, and maps to human chromosome 10q25.3.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   CREB3L3 is a 461 amino acid single-pass type II membrane protein that localizes to the endoplasmic reticulum (ER) and, in response to ER stress, is cleaved and translocated to the nucleus. Expressed exclusively in liver, CREB3L3 functions as a transcription factor that, during ER stress, is thought to activate genes that are involved in both the unfolded protein response and the acute phase response (APR). Additionally, CREB3L3 is underexpressed in hepatocellular carcinoma, suggesting a possible role as a tumor suppressor. CREB3L3 functions as a dimer and contains one leucine zipper domain, a KDEL-like sequence and a bZIP domain, through which it conveys its DNA binding ability. Three isoforms of CREB3L3 exist due to alternative splicing events.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11190R-A488)

Fournisseur:  Bioss
Description:   C9 is a plasma protein synthesized in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerization of 12-18 C9 molecules. These polymerized C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12259R-CY5)

Fournisseur:  Bioss
Description:   Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12259R-CY3)

Fournisseur:  Bioss
Description:   Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Cell adhesion molecules influence cell growth, differentiation, embryogenesis, immune response and cancer metastasis by networking information from the extracellular matrix to the cell. Sidekick-1 (SDK1) is a 2,213 amino acid single-pass membrane protein that functions as a cell adhesion molecule by guiding axonal terminals to specific synapses in developing neurons. Existing as three alternatively spliced isoforms, Sidekick-1 is expressed in retinal neurons and contains thirteen fibronectin type-III domains and six Ig-like C2-type (immunoglobulin-like) domains. Sidekick-1 expression is upregulated in glomeruli of patients with HIV-associated nephropathy, where it leads to podocyte dysfunction. The gene encoding Sidekick-1 maps to human chromosome 7p22.2 and murine chromosome 5 G2.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11110R-A680)

Fournisseur:  Bioss
Description:   Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDH17 is a 1159 amino acid single-pass type I membrane protein that contains six cadherin domains. Expressed as multiple alternatively spliced isoforms, PCDH17 is thought to function as a calcium-dependent cell adhesion protein that may play a role in establishing cell-cell connections within brain tissue. The gene encoding PCDH17 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome.
UOM:  1 * 100 µl
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