Votre recherche pour: barbs

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

Promotion

Numéro de catalogue: (PRSI36-346)

Fournisseur: ProSci Inc.

Description: VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.

UOM: 1 * 25 µG

Promotion

Numéro de catalogue: (BOSSBS-3848R-A680)

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 localises 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

Promotion

Numéro de catalogue: (BOSSBS-3848R-A555)

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

Promotion

Numéro de catalogue: (BOSSBS-3848R-CY5.5)

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

Promotion

Numéro de catalogue: (PRSI36-349)

Fournisseur: ProSci Inc.

Description: VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.

UOM: 1 * 100 µl

Promotion

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

Promotion

Numéro de catalogue: (BOSSBS-3848R-CY3)

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

Promotion

Numéro de catalogue: (BOSSBS-12445R-A350)

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

Promotion

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

Promotion

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

Promotion

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

Promotion

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

Promotion

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

Promotion

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

Promotion

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

Promotion