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Masterflex+Barb+Fittings
Numéro de catalogue:
(BOSSBS-3848R-HRP)
Fournisseur:
Bioss
Description:
Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3848R-A647)
Fournisseur:
Bioss
Description:
Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3848R-A488)
Fournisseur:
Bioss
Description:
Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0730R-A647)
Fournisseur:
Bioss
Description:
Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0730R-FITC)
Fournisseur:
Bioss
Description:
Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3848R-A350)
Fournisseur:
Bioss
Description:
Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.
UOM:
1 * 100 µl
Fournisseur:
Whatman products (Cytiva)
Description:
Ces capsules de filtrage pour les eaux souterraines Polycap™ GW (Ground Water) sont spécialement destinées à préparer des échantillons provenant des eaux souterraines avant l'analyse des métaux dissous. La conception intégrée, avec des raccords cannelés échelonnés et une membrane hydrophyle en polyéthersulfone (PES), en fait une méthode de prélévement facile à utiliser sur le terrrain.
Numéro de catalogue:
(BOSSBS-8256R)
Fournisseur:
Bioss
Description:
Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12445R)
Fournisseur:
Bioss
Description:
Caldesmon, Filamin 1, Nebulin, Plastin, ADF, Gelsolin, CapG, Dematin and Cofilin are differentially expressed Actin-binding proteins. Both muscular (CDh) and non-muscular (CD1) forms of Caldesmon bind to Actin as well as to Calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CD1 is widely expressed in non-muscle tissues and cells. CapG, also designated Actin-regulatory protein and macrophage-capping protein, is a macrophage-specific protein that reversibly blocks the barbed ends of Actin filaments, but does not sever preformed ones. The interactions of CapG with Actin may be important in the regulation of nuclear and cytoplasmic structures. CapG is a calcium-sensitive DNA-binding protein that plays a role in macrophage function. It is expressed in macrophages and macrophage-like cells and can localize both to the nucleus and the cytoplasm.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12445R-A647)
Fournisseur:
Bioss
Description:
Caldesmon, Filamin 1, Nebulin, Plastin, ADF, Gelsolin, CapG, Dematin and Cofilin are differentially expressed Actin-binding proteins. Both muscular (CDh) and non-muscular (CD1) forms of Caldesmon bind to Actin as well as to Calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CD1 is widely expressed in non-muscle tissues and cells. CapG, also designated Actin-regulatory protein and macrophage-capping protein, is a macrophage-specific protein that reversibly blocks the barbed ends of Actin filaments, but does not sever preformed ones. The interactions of CapG with Actin may be important in the regulation of nuclear and cytoplasmic structures. CapG is a calcium-sensitive DNA-binding protein that plays a role in macrophage function. It is expressed in macrophages and macrophage-like cells and can localize both to the nucleus and the cytoplasm.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12445R-CY5)
Fournisseur:
Bioss
Description:
Caldesmon, Filamin 1, Nebulin, Plastin, ADF, Gelsolin, CapG, Dematin and Cofilin are differentially expressed Actin-binding proteins. Both muscular (CDh) and non-muscular (CD1) forms of Caldesmon bind to Actin as well as to Calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CD1 is widely expressed in non-muscle tissues and cells. CapG, also designated Actin-regulatory protein and macrophage-capping protein, is a macrophage-specific protein that reversibly blocks the barbed ends of Actin filaments, but does not sever preformed ones. The interactions of CapG with Actin may be important in the regulation of nuclear and cytoplasmic structures. CapG is a calcium-sensitive DNA-binding protein that plays a role in macrophage function. It is expressed in macrophages and macrophage-like cells and can localize both to the nucleus and the cytoplasm.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0730R-CY5.5)
Fournisseur:
Bioss
Description:
Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal Alpha-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.
UOM:
1 * 100 µl
Fournisseur:
Avantor Fluid Handling
Description:
Compatible with Masterflex® L/S® or series Q drive.
Numéro de catalogue:
(516-8940)
Fournisseur:
Cytiva (Formerly Pall Lab)
Description:
Porte-filtre, Kit de joints de rechange, contient 5 joints en PTFE, 10 joints toriques Viton et 1 adaptateur pour embout de tuyau en acier inoxydable pour tubes de 6,4 mm de DI, Pour: Pressure filtration funnels, Acier inoxydable
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-12445R-CY7)
Fournisseur:
Bioss
Description:
Caldesmon, Filamin 1, Nebulin, Plastin, ADF, Gelsolin, CapG, Dematin and Cofilin are differentially expressed Actin-binding proteins. Both muscular (CDh) and non-muscular (CD1) forms of Caldesmon bind to Actin as well as to Calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CD1 is widely expressed in non-muscle tissues and cells. CapG, also designated Actin-regulatory protein and macrophage-capping protein, is a macrophage-specific protein that reversibly blocks the barbed ends of Actin filaments, but does not sever preformed ones. The interactions of CapG with Actin may be important in the regulation of nuclear and cytoplasmic structures. CapG is a calcium-sensitive DNA-binding protein that plays a role in macrophage function. It is expressed in macrophages and macrophage-like cells and can localize both to the nucleus and the cytoplasm.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12445R-A555)
Fournisseur:
Bioss
Description:
Caldesmon, Filamin 1, Nebulin, Plastin, ADF, Gelsolin, CapG, Dematin and Cofilin are differentially expressed Actin-binding proteins. Both muscular (CDh) and non-muscular (CD1) forms of Caldesmon bind to Actin as well as to Calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CD1 is widely expressed in non-muscle tissues and cells. CapG, also designated Actin-regulatory protein and macrophage-capping protein, is a macrophage-specific protein that reversibly blocks the barbed ends of Actin filaments, but does not sever preformed ones. The interactions of CapG with Actin may be important in the regulation of nuclear and cytoplasmic structures. CapG is a calcium-sensitive DNA-binding protein that plays a role in macrophage function. It is expressed in macrophages and macrophage-like cells and can localize both to the nucleus and the cytoplasm.
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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