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Masterflex+Barb+Fittings


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Numéro de catalogue: (BOSSBS-12524R-A680)

Fournisseur:  Bioss
Description:   Actin polymerization is required for a variety of cell functions, including chemotaxis, cell migration, cell adhesion, and platelet activation. Cells trigger actin polymerization through either the de novo nucleation of filaments from monomeric actin, the severing of existing filaments to create uncapped barbed ends, or the uncapping of existing barbed ends. The nucleation of actin is a rate-limiting and unfavorable reaction in actin polymerization and therefore requires the involvement of the Arp2/3 complex, which helps create new filaments and promotes the end-to-side cross-linking of actin filaments into the branching meshwork. The Arp2/3 complex consists of the actin-related proteins Arp2 and Arp3, and various other accessory proteins. The Arp2/3 complex promotes actin nucleation by binding the pointed end of actin filaments, or by associating with the side of an existing filament, and nucleates growth in the barbed direction. In addition, the Arp2/3 complex also mediates actin cytoskeletal outgrowths that are regulated by the Rho family of small GTPases. In response to GTP-binding Cdc42, the Arp2/3 complex binds the Cdc42 substrates, namely the WASP proteins, and initiates the formation of lamellipodia and filopodia.
UOM:  1 * 100 µl

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:  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:  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-A488)

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-5161R-CY5)

Fournisseur:  Bioss
Description:   F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
UOM:  1 * 100 µl
Fournisseur:  Cytiva (Formerly Pall Lab)
Description:   Supracap™ 100 depth filter capsules with PP housing are scalable capsules with Seitz® high performance depth filter media. They are suitable for process development and pilot scale applications.

Fournisseur:  ENZO LIFE SCIENCES
Description:   Cytochalasin D is a cell-permeable fungal toxin which binds to the barbed end of actin filaments inhibiting both the association and dissociation of subunits. It causes the disruption of actin filaments and inhibition of actin polymerization. It is about 10-fold more effective than cytochalasin B and does not inhibit monosaccharide transport across cell membranes. Inactivates low conductance K+ channels. Modulates CD4 cross-linking in T-lymphocytes and increases intracellular Ca2+ levels. Exhibits antitumor activity. Induces apoptosis.
UOM:  1 * 1 mg
New Product

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-4169R-A647)

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-4169R-A488)

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-5613R-CY5.5)

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-5613R-CY7)

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-5161R-A350)

Fournisseur:  Bioss
Description:   F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
UOM:  1 * 100 µl
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