Votre recherche pour: Hexafluoropropene+trimer

Numéro de catalogue: (BOSSBS-6459R-HRP)

Fournisseur: Bioss

Description: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-6459R-FITC)

Fournisseur: Bioss

Description: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-0886R-CY7)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-0886R-CY3)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-0886R-CY5)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-12354R)

Fournisseur: Bioss

Description: Hexon protein is a major coat protein of adenoviruses. Adenoviruses capsids have three principal protein components: the hexon, the penton, and the fiber. Hexon consists of three subunits together forming two major components of different morphological symmetry. A triangular top with three towers of density is superimposed on a more bulky pseudo hexagonal base. The symmetry of the top is in accord with the trimeric nature of hexon, but that of the base derives from the molecular function, which is to provide a densely packed impenetrable protective outer layer for the virion.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-1429R-CY3)

Fournisseur: Bioss

Description: GAI3 is the a subunit of inhibitory trimeric G protein (Gi), which inhibits adenylate cyclase once its G protein coupled receptors (GPCR) such as a2 adrenergic receptors are activated. GAI3 can be inactivated by pertussis toxin. Guanine nucleotide binding proteins are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor regulated K(+) channels.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9322R-CY3)

Fournisseur: Bioss

Description: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9322R-A750)

Fournisseur: Bioss

Description: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9322R-A647)

Fournisseur: Bioss

Description: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

UOM: 1 * 100 µl

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Numéro de catalogue: (SHBTPB-500-18)

Fournisseur: Shenandoah Biotechnology

Description: IL-2C126S, an immune-regulating cytokine originating from lymphocytes, operates via the IL-2R receptor to trigger the expansion of activated T cells and encourage T cell maturation. IL-2 mediates its action by binding to IL-2 receptors (IL-2R), consisting of either trimeric receptors made of IL-2Rα (CD25), IL-2Rβ (CD122), and IL-2Rγ (γc, CD132) chains or dimeric βγ IL-2Rs.

UOM: 1 * 1 KIT

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Numéro de catalogue: (BOSSBS-1429R-A647)

Fournisseur: Bioss

Description: GAI3 is the a subunit of inhibitory trimeric G protein (Gi), which inhibits adenylate cyclase once its G protein coupled receptors (GPCR) such as a2 adrenergic receptors are activated. GAI3 can be inactivated by pertussis toxin. Guanine nucleotide binding proteins are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor regulated K(+) channels.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-6459R-A680)

Fournisseur: Bioss

Description: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-6459R-A647)

Fournisseur: Bioss

Description: Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

UOM: 1 * 100 µl

Promotion

Numéro de catalogue: (BOSSBS-11726R-CY7)

Fournisseur: Bioss

Description: Hexosaminidase A (HEXA), also designated beta-Hexosaminidase A, is a trimer composed of one å chain, one ∫-A chain and one ∫-B chain and is found in the lysosomes of cells. HEXA, along with the cofactor CM2 activator protein, catalyzes the degradation of GM2 ganglioside and other molecules containing terminal N-acetyl hexosamines in the brain and other tissues. A mutation in the å subunit of hexosaminidase is the cause of Tay-Sachs disease (TSD), also known as GM2-gangliosidosis type I. TSD is a fatal autosomal recessive lysosomal storage disease of the central nervous system (CNS) caused by insufficient activity of the HEXA enzyme that results in a failure to process GM2 gangliosides. The accumulation of GM2 ganglioside in the absence of HEXA activity causes progressive destruction of the CNS.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-1961R-A750)

Fournisseur: Bioss

Description: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.

UOM: 1 * 100 µl

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