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Catalog Number: (BOSSBS-11261R-HRP)
Supplier: Bioss
Description: Syntaxins, a family of proteins involved in the fusion of synaptic vesicles with the plasma membrane, display broad tissue distribution and contain carboxy-terminal hydrophobic domains that direct themselves to their respective intracellular compartments. Synaptin 6 is a 255 amino acid protein that is widely expressed, with higher expression levels in brain, lung and kidney. This synaptin co-localizes with vesicle associated membrane protein (VAMP) 4 to tubular and vesicular membranes of the Golgi apparatus. The cytosolic domain of Syntaxin 6 reduces the rate on Glut4 reinternalization upon insulin withdrawl and is involved in a memrane-trafficking process that removes Glut4 from traffic directed to the plasma membrane. Syntaxin 6 is upregulated in activated macrophages in conjunction with an increase in the secretion of cytokines. The delivery of microdomain-associated lipids and proteins to the cell surface is regulated by Syntaxin 6.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11261R-CY5)
Supplier: Bioss
Description: Syntaxins, a family of proteins involved in the fusion of synaptic vesicles with the plasma membrane, display broad tissue distribution and contain carboxy-terminal hydrophobic domains that direct themselves to their respective intracellular compartments. Synaptin 6 is a 255 amino acid protein that is widely expressed, with higher expression levels in brain, lung and kidney. This synaptin co-localizes with vesicle associated membrane protein (VAMP) 4 to tubular and vesicular membranes of the Golgi apparatus. The cytosolic domain of Syntaxin 6 reduces the rate on Glut4 reinternalization upon insulin withdrawl and is involved in a memrane-trafficking process that removes Glut4 from traffic directed to the plasma membrane. Syntaxin 6 is upregulated in activated macrophages in conjunction with an increase in the secretion of cytokines. The delivery of microdomain-associated lipids and proteins to the cell surface is regulated by Syntaxin 6.
UOM: 1 * 100 µl


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Catalog Number: (BOSSBS-13629R-A647)
Supplier: Bioss
Description: Chloride channels (CLCs) regulate cellular traffic of chloride ions, a critical component of all living cells. CLCs are involved in membrane potential stabilization, signal transduction, cell volume regulation and organic solute transport. The putative 247 amino acid protein chloride intracellular channel 2 (CLIC2), also designated XAP121, shares 60% identity with the CLIC1 protein and demonstrates expression in only fetal liver and adult skeletal muscle tissues. The CLIC2 gene maps to chromosome Xq28 and contains 6 exons. Because a direct association exists between a number of human chloride channel genes and a range of hereditary diseases, CLIC2 is a potential candidate for one of the many diseases linked to Xq28. The hereditary form of incontinentia pigmenti (IP2), for example, is a rare disorder characterized by abnormalities of the tissues and organs derived from the ectoderm and neuroectoderm that has been linked to Xq28
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13694R-A488)
Supplier: Bioss
Description: NOSTRIN (nitric oxide synthase trafficker isoform 1), also known as endothelial nitric oxide synthase traffic inducer, is a member of the Pombe Cdc15 homology (PCH) family of proteins. NOSTRIN is expressed in the vascular endothelial cells of highly vascularized tissues such as placenta, lung, kidney and heart. It consists of an N-terminal Cdc15 domain with an FCH (Fes/CIP homology) region, two coiled coil domains and a C-terminal SH3 domain. NOSTRIN typically exists as a trimer. It functions as an adaptor protein binding to caveolin-1 via an internal domain and NOS3 via its SH3 domain, forming a ternary complex which facilitates caveolar transport of NOS3. The NOS3 protein is responsible for the production of nitric oxide (NO), a potent mediator in various biological processes. The translocation of NOS3 from the plasma membrane to intracellular vesicle-like structures diminishes NO production. NOSTRIN also interacts with Dynamin and N-WASP via its SH3 domain.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13495R-A488)
Supplier: Bioss
Description: The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells and is comprised of more than 100 different subunits. Many of the subunits belong to a family called nucleoporins (Nups), which are characterized by the presence of O-linked-N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). gp210, also known as Nup210 (nucleoporin 210kDa) or POM210, is a 1,887 amino acid single-pass type I membrane protein that localizes to both the endoplasmic reticulum and to the nucleus, specifically within the NPC. Expressed ubiquitously with highest expression in pancreas, testis, lung, ovary and liver, gp210 functions as a nucleoporin that is capable of dimerization and is essential for the assembly, fusion and structural integrity of the NPC. gp210 exists as multiple alternatively spliced isoforms and is subject to post-translational phosphorylation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13688R-A750)
Supplier: Bioss
Description: This gene encodes a scaffold protein that functions in the extracellular signal-regulated kinase (ERK) cascade. The protein is localized to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2. Studies of the orthologous gene in mouse indicate that it regulates late endosomal traffic and cell proliferation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. A pseudogene of this gene is located on the long arm of chromosome 13. [provided by RefSeq, Aug 2011]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13103R-CY5)
Supplier: Bioss
Description: Cycling proteins play important roles in the organization and function of the early secretory pathway by participating in membrane traffic and selective transport of cargo between the endoplasmic reticulum (ER), the intermediate compartment (ERGIC), and the Golgi. A family of membrane bound, ubiquitous proteins involved in the selective transport of newly synthesized glycoproteins from the ER to the ERGIC include VIP36, ERGIC-53, ERGIC-1, ERGIC-2 and ERGIC-3. ERGIC-1, also designated ERGIC32, is thought to modulate the activity of a complex formed by ERGIC-2, also designated Erv41, and ERGIC-3, also designated Erv46. ERGIC-2 and ERGIC-3 are both mammalian homologs of yeast proteins abundant in COPII-coated vesicles and localize to the Cis-face of the Golgi apparatus.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6703R-A350)
Supplier: Bioss
Description: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6703R-A555)
Supplier: Bioss
Description: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12922R-HRP)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-12922R-A555)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-12922R-CY3)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-12922R-CY5)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-12922R-CY7)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-13688R-HRP)
Supplier: Bioss
Description: This gene encodes a scaffold protein that functions in the extracellular signal-regulated kinase (ERK) cascade. The protein is localized to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2. Studies of the orthologous gene in mouse indicate that it regulates late endosomal traffic and cell proliferation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. A pseudogene of this gene is located on the long arm of chromosome 13. [provided by RefSeq, Aug 2011]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13103R-CY7)
Supplier: Bioss
Description: Cycling proteins play important roles in the organization and function of the early secretory pathway by participating in membrane traffic and selective transport of cargo between the endoplasmic reticulum (ER), the intermediate compartment (ERGIC), and the Golgi. A family of membrane bound, ubiquitous proteins involved in the selective transport of newly synthesized glycoproteins from the ER to the ERGIC include VIP36, ERGIC-53, ERGIC-1, ERGIC-2 and ERGIC-3. ERGIC-1, also designated ERGIC32, is thought to modulate the activity of a complex formed by ERGIC-2, also designated Erv41, and ERGIC-3, also designated Erv46. ERGIC-2 and ERGIC-3 are both mammalian homologs of yeast proteins abundant in COPII-coated vesicles and localize to the Cis-face of the Golgi apparatus.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
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