71 Results for: "talk"

Supplier: Corning

These 96-well solid black and white polystyrene microplates are designed to reduce well-to-well cross-talk.

Supplier: Thermo Fisher Scientific

PS, 96 wells per frame. For fluorescence/luminescence-based immunoassays and binding assays, these modules have been designed using the standard 96 MicroWell™ LockWell™ format. Opaque white modules have a reflective surface and offer low cross talk and minimal background. Opaque black modules with light absorbing surface offer minimum cross talk and back scattered light.

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganisation in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Corning

With their proprietary design, these microplates are ideal for generating and analyzing 3D multicellular spheroids in the same microplate. The Ultra-Low Attachment (ULA) surface enables uniform and reproducible 3D multicellular spheroid formation. The black opaque microplate body shields each optically clear, round bottom well from well-to-well cross-talk.

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganisation in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.

Supplier: ProSci Inc.

Junctional complexes between the plasma membrane and endoplasmic/sarcoplasmic reticulum are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. JPH1 is a component of junctional complexes and is composed of a C-terminal hydrophobic segment spanning the endoplasmic/sarcoplasmic reticulum membrane and a remaining cytoplasmic domain that shows specific affinity for the plasma membrane.Junctional complexes between the plasma membrane and endoplasmic/sarcoplasmic reticulum are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. The protein encoded by this gene is a component of junctional complexes and is composed of a C-terminal hydrophobic segment spanning the endoplasmic/sarcoplasmic reticulum membrane and a remaining cytoplasmic domain that shows specific affinity for the plasma membrane. This gene is a member of the junctophilin gene family.

Supplier: Bioss

ARFIP2 is a ubiquitously expressed protein implicated in mediating cross talk between RAC and ARF small GTPases. It has been shown that ARFIP2 binds specifically to GTP-bound ARF1 and ARF6, but binds to Rac-GTP and Rac-GDP with similar affinities. The X-ray structure of arfaptin reveals an elongated, crescent-shaped dimer of 3-helix coiled-coils. Structures of arfaptin with Rac bound to either GDP or the slowly hydrolysable analog GMPPNP show that the switch regions adopt similar conformations in both complexes.