Procurou por: Brefeldin+A

Fornecedor: Cayman Chemical

Descrição: Brefeldin A

Fornecedor: Thermo Fisher Scientific

Descrição: Brefeldin A (natural)

MSDS

Fornecedor: TCI

Descrição: Brefeldin A ≥98.0% (by HPLC)

Código de Artigo: (APOSBIB3042-50MG)

Fornecedor: Apollo Scientific

Descrição: BFA is a macrolide antiobiotic. Disrupts mechanism of Golgi apparatus.

UOM: 1 * 50 mg

Promoção

Fornecedor: ENZO LIFE SCIENCES

Descrição: GEF inhibitor

Novo produto

Código de Artigo: (BOSSBS-11804R-CY3)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-11804R-FITC)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12866R-A555)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-11804R-A750)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insensitive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12866R-A750)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insensitive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-11804R-A350)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12866R-A488)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12866R)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12866R-A350)

Fornecedor: Bioss

Descrição: Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12922R-A488)

Fornecedor: Bioss

Descrição: The ADP-ribosylation factor (Arf) family comprises a group of structurally and functionally conserved 21 kDa proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. Arf is involved in intracellular protein traffic to and within the Golgi complex. Arf has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. Like other small GTPases, Arf is found to be active when bound to GTP and inactive when bound to GDP. Arf’s activation is dependent upon guanine nucleotide exchange factors (GEFs) which increase the rate of exchange of bound GDP with GTP. All GEFs have a highly conserved Sec7 domain. GEF activity lies in the Sec7 domain and this activity has been shown to be inhibited by the fungal metabolite brefeldin-A (BFA). A small group of GEFs which are insensitive to brefeldin-A (BFA) include cytohesin-1 (B2-1), cytohesin-2 (ARNO), cytohesin-3 (ARNO3), and cytohesin-4. All cytohesins function in the cell periphery and contain a pleckstrin homology (PH) domain. The PH domain has been shown to interact with phosphatidylinositol 3,4,5-triphosphate and is believed to promote membrane targeting of the cytohesins. Recruitment of the cytohesins to the membranes can occur in response to tyrosine kinase receptor activation. This response appears to require the activation of phosphatidylinositol 3-kinase (PI 3-kinase).

UOM: 1 * 100 µl

Promoção

Código de Artigo: (BOSSBS-12922R-A750)

Fornecedor: Bioss

Descrição: The ADP-ribosylation factor (Arf) family comprises a group of structurally and functionally conserved 21 kDa proteins, which are members of the Ras superfamily of regulatory GTP-binding proteins. Arf is involved in intracellular protein traffic to and within the Golgi complex. Arf has a number of disparate activities including maintenance of organelle integrity, assembly of coat proteins, as a co-factor for cholera toxin and as an activator of phospholipase D. Like other small GTPases, Arf is found to be active when bound to GTP and inactive when bound to GDP. Arf's activation is dependent upon guanine nucleotide exchange factors (GEFs) which increase the rate of exchange of bound GDP with GTP. All GEFs have a highly conserved Sec7 domain. GEF activity lies in the Sec7 domain and this activity has been shown to be inhibited by the fungal metabolite brefeldin-A (BFA). A small group of GEFs which are insensitive to brefeldin-A (BFA) include cytohesin-1 (B2-1), cytohesin-2 (ARNO), cytohesin-3 (ARNO3), and cytohesin-4. All cytohesins function in the cell periphery and contain a pleckstrin homology (PH) domain. The PH domain has been shown to interact with phosphatidylinositol 3,4,5-triphosphate and is believed to promote membrane targeting of the cytohesins. Recruitment of the cytohesins to the membranes can occur in response to tyrosine kinase receptor activation. This response appears to require the activation of phosphatidylinositol 3-kinase (PI 3-kinase).

UOM: 1 * 100 µl

Promoção