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acids+and+salts+high+purity
Numéro de catalogue:
(BOSSBS-12574R-A555)
Fournisseur:
Bioss
Description:
p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11210R-FITC)
Fournisseur:
Bioss
Description:
Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH9 (Dynein, axonemal, heavy chain 9), also known as DYH9, HL20, DNEL1, Dnahc9 or DNAH17L, is a member of the Dynein heavy chain family and comprises one of the heavy chain subunits of axonemal Dynein. DNAH9 consists of an N-terminal stem which is responsible for interacting with other Dynein components and binding cargo, and four P-loops that comprise the motor domain at its C-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7342R-CY7)
Fournisseur:
Bioss
Description:
The Sp transcription factor family includes Sp1, Sp2, Sp3 (SPR-2) and Sp4 (SPR-1). Sp transcription factors share similar structures but do not share simi-lar functions. All four proteins contain a highly conserved DNA-binding domain composed of three zinc fingers at the C-terminus. Sp family members bind the consensus sequence GGGGCGGGGC and other closely related sequences which are known as GC boxes. Sp1, Sp3 and Sp4 share a high affinity for GC boxes while Sp2 does not. Sp2 only weakly binds to GT boxes. Sp1, Sp2 and Sp3 are ubiquitously expressed, while Sp4 is abundantly expressed in brain with limited expression in other tissues. Sp1 and Sp3, but not Sp2 or Sp4, interact with E2, a regulatory element for the ∫4 subunit of neuronal nicotinic acetylcholine receptors. Sp3 is the only Sp member to inhibit Sp1 and Sp4 media
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7342R-A647)
Fournisseur:
Bioss
Description:
The Sp transcription factor family includes Sp1, Sp2, Sp3 (SPR-2) and Sp4 (SPR-1). Sp transcription factors share similar structures but do not share simi-lar functions. All four proteins contain a highly conserved DNA-binding domain composed of three zinc fingers at the C-terminus. Sp family members bind the consensus sequence GGGGCGGGGC and other closely related sequences which are known as GC boxes. Sp1, Sp3 and Sp4 share a high affinity for GC boxes while Sp2 does not. Sp2 only weakly binds to GT boxes. Sp1, Sp2 and Sp3 are ubiquitously expressed, while Sp4 is abundantly expressed in brain with limited expression in other tissues. Sp1 and Sp3, but not Sp2 or Sp4, interact with E2, a regulatory element for the ∫4 subunit of neuronal nicotinic acetylcholine receptors. Sp3 is the only Sp member to inhibit Sp1 and Sp4 media
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7342R-FITC)
Fournisseur:
Bioss
Description:
The Sp transcription factor family includes Sp1, Sp2, Sp3 (SPR-2) and Sp4 (SPR-1). Sp transcription factors share similar structures but do not share simi-lar functions. All four proteins contain a highly conserved DNA-binding domain composed of three zinc fingers at the C-terminus. Sp family members bind the consensus sequence GGGGCGGGGC and other closely related sequences which are known as GC boxes. Sp1, Sp3 and Sp4 share a high affinity for GC boxes while Sp2 does not. Sp2 only weakly binds to GT boxes. Sp1, Sp2 and Sp3 are ubiquitously expressed, while Sp4 is abundantly expressed in brain with limited expression in other tissues. Sp1 and Sp3, but not Sp2 or Sp4, interact with E2, a regulatory element for the ∫4 subunit of neuronal nicotinic acetylcholine receptors. Sp3 is the only Sp member to inhibit Sp1 and Sp4 media
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12550R-CY5)
Fournisseur:
Bioss
Description:
Mitochondrial ATP synthases (ATPases) transduce the energy contained in membrane electrochemical proton gradients into the energy required for synthesis of high-energy phosphate bonds. ATPases contain two linked complexes: F1, the hydrophilic catalytic core; and F0, the membrane-embedded protein channel. F1 consists of three Alpha chains and three Beta chains, which are weakly homologous, as well as one Gamma chain, one Delta chain and one Gamma chain. F0 consists of three subunits: a, b and c. A mitochondrial F1-ATPase inhibitor protein, ATPIF1 (ATPase inhibitory factor 1), also known as IP, IF1, ATPI or ATPIP (ATPase inhibitor protein), binds to the C-terminal region of a Beta subunit of the F1-ATPase at low pH values and, via interference of the Beta and Gamma subunit interaction, ATPIF1 regulates the activity of the F1F0-ATPase. This reversible ATPIF1 binding to F1F0-ATPase also occurs on the surface of endothelial cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11210R-CY7)
Fournisseur:
Bioss
Description:
Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH9 (Dynein, axonemal, heavy chain 9), also known as DYH9, HL20, DNEL1, Dnahc9 or DNAH17L, is a member of the Dynein heavy chain family and comprises one of the heavy chain subunits of axonemal Dynein. DNAH9 consists of an N-terminal stem which is responsible for interacting with other Dynein components and binding cargo, and four P-loops that comprise the motor domain at its C-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12574R-CY5)
Fournisseur:
Bioss
Description:
p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12574R-CY7)
Fournisseur:
Bioss
Description:
p130 represents one of several known substrates for v-Crk encoded p47. p130 Cas (for Crk-associated substrate) exhibits a high level of tyrosine phosphorylation and is tightly associated with v-Crk, suggesting a role in v-Crk-mediated cell signaling. The molecular cloning of p130 Cas has shown it to represent a novel SH3 containing signaling molecule with a cluster of multiple putative SH2-binding motifs for v-Crk. By immunoprecipitation analysis, p130 Cas has been shown to be highly phosphorylated at tyrosine residues subsequent to either v-Src p60 or v-Crk-mediated transformation and to form stable complexes with both of these transforming proteins. p130 Cas behaves as an extremely potent substrate for protein tyrosine kinases and has been reported to relocate from the cytoplasm to cell membrane upon tyrosine phosphorylation. One proposed model is that the SH2 domain of v-Crk functions to activate c-Src kinase, which in turn phosphorylates p130 Cas.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11210R-CY3)
Fournisseur:
Bioss
Description:
Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH9 (Dynein, axonemal, heavy chain 9), also known as DYH9, HL20, DNEL1, Dnahc9 or DNAH17L, is a member of the Dynein heavy chain family and comprises one of the heavy chain subunits of axonemal Dynein. DNAH9 consists of an N-terminal stem which is responsible for interacting with other Dynein components and binding cargo, and four P-loops that comprise the motor domain at its C-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11210R-CY5)
Fournisseur:
Bioss
Description:
Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. DNAH9 (Dynein, axonemal, heavy chain 9), also known as DYH9, HL20, DNEL1, Dnahc9 or DNAH17L, is a member of the Dynein heavy chain family and comprises one of the heavy chain subunits of axonemal Dynein. DNAH9 consists of an N-terminal stem which is responsible for interacting with other Dynein components and binding cargo, and four P-loops that comprise the motor domain at its C-terminus.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3619R-CY3)
Fournisseur:
Bioss
Description:
Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 70 kDa, which is identified as CD86 (HLDA V; WS Code BP BP072. HLDA V; WS Code A A109. HLDA VI; WS Code BP 95. HLDA VI; WS Code B CD86.9). CD86 is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors. It is expressed at high levels on resting peripheral monocytes and dendritic cells and at very low density on resting B and T lymphocytes. CD86 expression is rapidly upregulated by B cell specific stimuli with peak expression at 18 to 42 hours after stimulation. CD86, along with CD80/B71, is an important accessory molecule in T cell co-stimulation via its interaction with CD28 and CD152/CTLA4. Since CD86 has rapid kinetics of induction, it is believed to be the major CD28 ligand expressed early in the immune response. It is also found on malignant Hodgkin and Reed Sternberg (HRS) cells in Hodgkin's disease.
Fournisseur:
JULABO GmbH
Description:
Grâce à la grande qualité de leurs matériaux et composants, les bains-marie en acier inoxydable PURA sont fonctionnels, et fiables pour les opérations de routine. Les bains-marie PURA sont faciles à utiliser; ils offrent un certain nombre de fonctions et de fonctionnalités qui permettent une utilisation efficace en laboratoire.
Numéro de catalogue:
(BOSSBS-6991R-A488)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6991R-A350)
Fournisseur:
Bioss
Description:
In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signaling between transcriptional activators and initiation factors. These complexes include the thyroid hormone receptor-associated protein (TRAP) complex, which interacts with thyroid receptors (TR), vitamin D receptors and other steroid receptors to facilitate hormone induced transcriptional activation. The TRAP complex consists of numerous proteins ranging in size including TRAP95, TRAP100, TRAP150, TRAP220 and TRAP230, that are characterized by the presence of a nuclear receptor recognition motif which mediates the ligand-dependent binding of TRAP proteins to the nuclear receptors. TRAP220 and TRAP100 are widely expressed and most abundantly detected in skeletal muscle, heart and placenta. TRAP95, TRAP150 and TRAP230 facilitate TR induced transcription by associating with an additional transcriptional coactivating complex SMCC (SRB and MED protein cofactor complex), which consists of various subunits that share homology with several components of the yeast transcriptional mediator complexes.
UOM:
1 * 100 µl
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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