Sie suchten nach: Klonier-Kits+und+Ligation


133'433  results were found

SearchResultCount:"133433"

Sort Results

Listenansicht Easy View

Bewerten Sie das Suchergebnis

Artikel-Nr: (BOSSBS-5164R-A555)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-5164R-A555
Beschreibung: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation.
UOM: 1 * 100 µl


Artikel-Nr: (BOSSBS-1677R-A750)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-1677R-A750
Beschreibung: Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
UOM: 1 * 100 µl


Neue Transparenz für europäische Kunden

Haben Sie an der Kasse unsere neue und verbesserte Sichtbarkeit des Lagerbestands bemerkt?

Weitere Informationen

Erweiterung der Lagerstandorte

Lieferant: Biotium
Beschreibung: CD309, also known as VEGFR2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGFR2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGFR2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGFR2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.

Artikel-Nr: (BTIUBNUM0721-50)
Lieferant: Biotium
Hersteller Artikel Nummer : BNUM0721-50
Beschreibung: CD309, also known as VEGFR2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGFR2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGFR2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGFR2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.
UOM: 1 * 50 µl


Lieferant: Biotium
Beschreibung: CD309, also known as VEGF-R2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGF-R2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGF-R2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGF-R2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.

Lieferant: ENZO LIFE SCIENCES
Beschreibung: CD40 is a 45-50 kDa type I membrane protein and a member of the tumor necrosis factor (TNF) receptor superfamily. CD40 is also known as pb50 or CDW40.  CD40 is expressed primarily by professional antigen-presenting cells and it is also expressed on non-immune cell types. The CD40 expressed by professional antigen-presenting cells plays a critical role in co-stimulation and antigen-presenting cell activation in T cell-dependent immune responses. Signals generated through CD40 in B cells are anti-apoptotic. These signals are also required for T cell-dependent B cell activation and proliferation, isotype switching, up-regulation of costimulatory receptors, germinal center formation and memory generation. CD40 signal transduction is initiated by binding trimeric CD40 ligand (CD40L) which is found on the surface of activated T cells.  CD40 engages several signalling pathways in B cells and these include NF-kB, the mitogen-activated protein kinases p38 and c-Jun N-terminal kinase. The 62 amino acid cytoplasmic domain (CD40c) of CD40 contains two linear TNF-receptor associated factor (TRAF) binding domains. The membrane proximal site of CD40c binds TRAF6 and the membrane distal site binds TRAF1, 2 and 3. CD40c is thought to mediate the CD40-dependant signalling pathways by recruitment of TRAF to this multimerized domain. CD40 ligation has also been shown to stimulate iNOS expression, and therefore NO production, by activating NF-kB in IFN-g treated microglial cells. NO derived from microglia has been implicated in the damage of myelin-producing oligodendrocytes in demyelinating disorders like multiple sclerosis (MS) and neuronal death during Alzheimer’s disease and brain trauma. Increased CD40-CD40 ligation has been implicated in the pathogenesis of several autoimmune inflammatory diseases, such as MS, arthritis and insulin-dependant diabetes.

New Product

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7 (Workshop IV; Code T155). CD7 is a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7 (also known as gp40, Leu9). CD7 is a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Artikel-Nr: (BOSSBS-5164R-CY5.5)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-5164R-CY5.5
Beschreibung: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation.
UOM: 1 * 100 µl


Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7 (Workshop IV; Code T155). CD7 is a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Lieferant: Biotium
Beschreibung: Recognizes a protein of 40 kDa, identified as CD7, a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

Artikel-Nr: (BOSSBS-5164R-A647)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-5164R-A647
Beschreibung: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. May also act as a negative regulator of ETS1 and may inhibit nuclear factor-kappa-B activation.
UOM: 1 * 100 µl


Inquire for Price
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das call noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 044 745 13 13.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das call noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 044 745 13 13.
Dieses Produkt kann nur an eine Lieferadresse versandt werden die über die entsprechende Lizenzen verfügt. Für weitere Hilfe bitte kontaktieren Sie Regulatory Affairs.
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
Das Produkt kann nicht in den Warenkorb gelegt werden.
Der Grund kann ein Preis auf Anfrage oder ein Artikelblock sein.
Bitte kontaktieren Sie Ihr zuständiges VWR Team für weitere Informationen
Dieses Produkt ist Ersatz für den von Ihnen gewünschten Artikel.
Mit diesem Symbol gekennzeichnete Produkte werden nicht mehr angeboten - bis zum Ende des Lagerbestands verkauft. Alternativen können durch Suchen mit der oben aufgeführten VWR-Katalognummer verfügbar sein. Wenn Sie weitere Hilfe benötigen, rufen Sie bitte den VWR-Kundendienst an unter 044 745 13 13
97 - 112 of 133'433
no targeter for Bottom