3044 Results for: "AMARELL, ARNO&amp"

Supplier: US Biological

Anti-CYTH2 Mouse Monoclonal Antibody [clone: 6H5]

Supplier: US Biological

Anti-CYTH2 Rabbit Polyclonal Antibody (Biotin)

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Merck

AMP (2-Amino-2-methylpropanol) for synthesis, Sigma-Aldrich®

Supplier: VWR Chemicals

5% water has been added to maintain liquidity at room temperature.

Supplier: Thermo Fisher Scientific

Adenosine-5'-monophosphoric acid (AMP) 99%

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol) 99%

Supplier: Thermo Fisher Scientific

AMP (2-Amino-2-methylpropanol), (max. 5% H₂O) 95%

Supplier: TCI

Adenosine-5'-monophosphoric acid (AMP) ≥98.0% (by HPLC, titration analysis)

Supplier: LIOFILCHEM

Antibiotic Tests, Ampicillin AMP 2 µg

Supplier: Apollo Scientific

Adenosine 5'-monophosphate monohydrate ≥96%

Supplier: TCI

AMP (2-Amino-2-methylpropanol) ≥93.0% (by GC, titration analysis)

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Apollo Scientific

Used for the preparation of buffer solutions, suitable for the determination of alkaline phosphatase.

Supplier: US Biological

Anti-AMP Activated Protein Kinase 1, 2 Rabbit Polyclonal Antibody

Supplier: US Biological

Anti-Cyclic AMP Rabbit Polyclonal Antibody

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Bioss

AMP deaminase plays a critical role in energy metabolism.Involvement in diseaseDefects in AMPD3 are the cause of adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE); also known as erythrocyte AMP deaminase deficiency. AMPDDE is a metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.

Supplier: Thermo Fisher Scientific

a useful ligand determinant that facilitate the binding of APS reductase inhibitors and activates adenosine receptor agonists.