"single-use assemblies"

Supplier: HONEYWELL SAFETY

Panoramasque is a full face mask dedicated to offer respiratory protection, depending on the canister type assembled on it. For optimal protection, it is recommended to use aluminium or plastic Honeywell (Sperian) filters. They can only be used in sufficiently ventilated premises where the atmosphere contains a minimum oxygen volume of 17%.

Supplier: HONEYWELL SAFETY

Optifit is a reusable, APR class 2 full face mask dedicated to offer respiratory protection, depending on the filter type assembled on it. For optimal protection it is recommended to use aluminium or plastic filters (Class 2). They can only be used in sufficiently ventilated premises where the atmosphere contains a minimum oxygen volume of 17%.

Supplier: BUCHI

AutoDest sensor. incl. cap nut, seal GL14, for automatic distillation, measures temperature of cooling media; for use with the Interface I-300/I-300 Pro and glass assembly V, S and E, För: Rotavapor®

Supplier: Corning

These tips are manufactured to stringent specifications under strict process controls and assembled via automation to ensure consistent performance and quality. Designed for use in Molecular devices FLIPR tetra automation systems.

Supplier: Trajan Scientific and Medical

Micro Extraction by Packed Sorbent (MEPS™) is a new development in the field of sample preparation by SPE (solid phase extraction). The MEPS™ product consists of two parts, the MEPS™ syringe and the MEPS™ Barrel Insert and Needle assembly (BIN). The MEPS™ approach to sample preparation is suitable for reversed phases, normal phases, mixed mode and ion exchange chemistries. Because MEPS™ BINs can be used for sample volumes as small as 10 µl it makes them particularly well suited to on-line use with LC-MS analysis of volume limited samples.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: ProSci Inc.

Tissue Factor (TF) is a single-pass type I membrane glycoprotein member of the tissue factor family. TF expression is highly dependent upon cell type. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. TF initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: Bioss

Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

Supplier: Avantor Fluid Handling

OmniTop Sample Tubes® are a convenient device that can be used to obtain fluid samples. Each OmniTop tube comes with a pre-attached 0,2 µm vent filter and 18" of tubing (C-Flex®, TYGON®, silicone or PharMed®).

Supplier: Bioss

C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants

Supplier: Bioss

C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants

Supplier: Bioss

EphB1, previously known as Elk (eph like kinase), is a receptor tyrosine kinase of the highly tissue restricted family of eph proteins. EphB1 and other ephB family members are type 1 membrane spanning proteins, comprised of immunoglobulin, fibronectin type III, and cysteine rich subdomains in the ecto domain, and the single uninterrupted cytoplasmic tyrosine kinase domain upstream of a carboxyterminal sterile alpha motif (SAM) domain. EphB family proteins bind ephrins of the B class. EphB1 is expressed predominately in developing neural structures in embryos, and in vascular epithelium of kidney, and other tissues. Upon binding to alternatively oligomerized ephrin B1, EphB1 signals regulation of cell attachment and cell to cell assembly. Members of this protein family are implicated in neuronal and vascular cell targeting.