827 Risultati per: "Masks"

Supplier: UVEX

The Uvex silv-Air premium product line comprises classic, white folding respirators that adapt to different face shapes. The headband and integrated sealing lip in all protection classes mean the masks are easy to put on correctly as well as making them comfortable to wear, even for extended periods.

Supplier: UVEX

All masks of the uvex silv-Air e family combine our unique technologies of optimum wearer comfort with extremely low breathing resistance. The products are therefore suitable for heavy work and for being worn for long periods of time. The increased size of the filter surface even enables the high-performance models to be worn for several days.

Supplier: 3B Scientific

This easy to transport torso allows the practice of adult CPR techniques. Optionally child CPR can also be practiced by changing the supplied springs inside the torso. Individual student face masks with a one-way non-rebreathing valve and disposable airways provide maximum protection against cross-contamination.

Supplier: VWR Collection

BEARD MASK COLOR: BLUE SIZE: 46CM DESCRIPTION: DETECTABLE, WITH EARLOOP, LATEXFREE ELASTIC MATERIAL: POLYPROPYLENE THICKNESS: 10-12 G/M PACKAGING: 100 PCS/BAG, 1000 PCS/CARTON 1 * 1.000 pezzi

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: Bioss

Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).

Supplier: VARIAN

Due to the methyl group and subsequent low carbon load, Bond Elut™ C1 is the least retentive of all alkyl group bonded phases for non-polar compounds. However, due to the extensive end capping of this sorbent to mask polar silanol activity, retention and elution of polar and multi-functional analytes can still be achieved. Typical applications include plasma, urine and aqueous samples.

Supplier: Dräger

The powered air-purifying respirator (PAPR) X-plore 8000 offers a number of user friendly standard and specialised carrying systems for standard and decontamination applications. Dräger has also developed a wide range of tight- and loose-fitting headgear such as half and full-face masks, short and long hoods and helmets with visor and protective visor. Standard and enhanced flexibility hoses are available and compatibility is ensured. Modular components: A wide range of components for every application.

Supplier: G-Biosciences

PAGE-Optimizer™ is a unique, spin column for the preparation of samples for SDS-PAGE. The columns contain a proprietary separation matrix that removes contaminants such as salts, detergents, cellular agents and other common buffering agents. PAGE-Optimizer™ helps eliminate smeared lanes, distorted and/ or smiling bands and swollen lanes. PAGE-Optimizer™ has also been shown to reveal protein bands previously masked by the above interfering agents.

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).