Wyszukano: Brefeldin+A

Numer katalogowy: (SIALB5936-200UL)

Producent: Merck

Opis: Brefeldin A produced from <i>Penicillium brefeldianum</i> may be used to study protein and lipid transport between Golgi complex and the cell surface.

j.m.: 1 * 200 µl

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Numer katalogowy: (BOSSBS-12922R-A647)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Producent: MP Biomedicals

Opis: Storage: Store at -20 °C.
Brefeldin A is a fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity. Produced by Penicillium brefeldianum. Blocks binding of the cytosolic coat protein b-COP and ARF to Golgi membranes mediated by protein G. Also blocks protein transportation into post-Golgi compartments. It activates the sphingomyelin cycle. Brefeldin A mediated apoptosis has been observed in human tumor cells.
Brefeldin A reversibly inhibits the intracellular translocation of proteins in eukaryotes, e.g., during transport of proteins to the cell surface for secretion or expression. It has been reported to block the response of cultured cells to cholera toxin. In HepG2 cells, BFA induces two blocks in the secretory pathway; one at the level of the endoplasmic reticulum-Golgi juncture and the other in the trans-Golgi network. Brefeldin A is used in the studies of Brefeldin A-inhibited Guanine Nucleotide-exchange Protein, BIG2, Regulates the Constitutive Release of TNFR1 Exosome-like Vesicles.
Brefeldin A (BFA) is a fungal metabolite which disrupts the structure and function of the Golgi apparatus. BFA is an activator of the sphingomyelin cycle. Brefeldin A-mediated apoptosis has been observed in human tumor cells.

Numer katalogowy: (BOSSBS-11804R-CY5)

Producent: Bioss

Opis: 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.

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12866R-CY7)

Producent: Bioss

Opis: 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.

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-FITC)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-11804R-HRP)

Producent: Bioss

Opis: 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.

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12866R-HRP)

Producent: Bioss

Opis: 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.

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-A555)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-CY3)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-HRP)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-CY5)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-CY7)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (BOSSBS-12922R-A680)

Producent: Bioss

Opis: 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).

j.m.: 1 * 100 µl

Wyprzedaż

Numer katalogowy: (PRSI55-082)

Producent: ProSci Inc.

Opis: The protein encoded by this gene is a peripheral membrane protein localized to the trans-Golgi network. It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. Alternative splicing results in multiple transcript variants.

j.m.: 1 * 400 µl

New Product Wyprzedaż

Numer katalogowy: (PRSI56-778)

Producent: ProSci Inc.

Opis: The protein encoded by this gene is a peripheral membrane protein. It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. It may play a role in the organization of trans-Golgi network subcompartment involved with membrane transport. [provided by RefSeq].

j.m.: 1 * 400 µl

New Product Wyprzedaż