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Masterflex+Barb+Fittings
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.
Fournisseur:
Cytiva (Formerly Pall Lab)
Description:
These are scaleable depth capsules for prefiltration and clarification. They are designed for small-volume production and scale-up evaluation.
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
Numéro de catalogue:
(BUCH037642)
Fournisseur:
BUCHI
Description:
Set of hose barbs, GL14, incl. 4× hose barb straight and 4× cap nut, Pour: Rotavapor® R-210 / R-215
UOM:
1 * 1 SET
Numéro de catalogue:
(MFLX77250-69)
Fournisseur:
Avantor Fluid Handling
Description:
Get the most out of your Masterflex® L/S® High-Performance Pump Head with these replacement parts.
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-0730R-A750)
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 stabilise 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 localised to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilise 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-A488)
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-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
Numéro de catalogue:
(BOSSBS-12445R-CY3)
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
Fournisseur:
Avantor Fluid Handling
Description:
Get the most our of your Masterflex® L/S® Easy-Load® II Pump Head with these replacement parts.
Numéro de catalogue:
(MFLX77200-07)
Fournisseur:
Avantor Fluid Handling
Description:
Make the most of your Masterflex drives replacement parts and other accessories.
UOM:
1 * 1 ST
Fournisseur:
Avantor Fluid Handling
Description:
Ultra low spallation protects fluid purity – ideal for sensitive and costly fluids and for filtration applications.
Fournisseur:
JOUR RESEARCH (VICI)
Description:
Barbed adapter, M10 × 1 thread, for 8 mm I.Ø tubing, PA
Numéro de catalogue:
(MFLX96423-92)
Fournisseur:
Avantor Fluid Handling
Description:
Ensure optimal performance from your Masterflex® B/T series pump.
UOM:
1 * 100 Voet
Numéro de catalogue:
(BOSSBS-0730R-CY3)
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
Appel de prix
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 est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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