51445 Résultats pour : "EVA PAPR"

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: US Biological

Anti-MPZL2 Rabbit Polyclonal Antibody (APC (Allophycocyanin))

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: THERMO MATRIX TECHNOLOGIES

Les produits CapMats et CapStrips Matrix sont conçus pour assurer une forte étanchéité à tout moment sur les tubes, microplaques et blocs Deep Well (à puits profonds). CapMats maintient l'étanchéité jusqu'à –80 °C, tandis que CapStrips permet de sceller individuellement les bouchons et les lignes.

Supplier: US Biological

Anti-MPZL2 Rabbit Polyclonal Antibody

Supplier: 3M

Le kit de démarrage TR-819 E pour unité filtrante à sécurité intrinsèque est prêt à l'emploi: il comporte toutes les pièces nécessaires pour se servir immédiatement de l'appareil.

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene.

Supplier: 3M

Le Versaflo™ Turbo TR-600 à ventilation assistée est un système de purification de l'air monté sur une ceinture. Lorsqu'il est utilisé avec l'une des pièces faciales 3M approuvées, il constitue un système à alimentation électrique pour la protection respiratoire contre les particules, les odeurs gênantes (le cas échéant), les gaz et les vapeurs.

Supplier: HONEYWELL SAFETY

Heavy duty air hoods range designed for use with powered air purifying respirator (PAPR) as Compact Air 200, Compact Air and Compact Air. This model offers protection to the head, the shoulders and the neck. It is equipped with full safety helmet. This system procures air to the user via the supply hose connected between PAPR (equipped with filters) and the hood. The filtered airflow enters by the front of the hood and leaves the hood via the face collar or the neck bib.

Supplier: RPB SAFETY

The RPB Z4 w/ PX5 PAPR starter kit provides everything needed to perform industrial welding and grinding tasks with the utmost in safety but also now with unmatched comfort and further reduced cost in use.

Supplier: ELTEN

Sporty ladies safety shoes made from nubuck leather combined with mesh inserts, skin-friendly textile lining, a full padded bellows tongue, collar padding, heel loop, and a dual-density rubber/EVA jo_SPORTY sole (oil, fuel and chemical resistant, temperature resistant from approx. -20 and +200 °C).

Supplier: RPB SAFETY

The RPB PX5 is a battery powered air purifying respirator fan unit which draws in contaminated air from the wearer's immediate vicinity, passing it through internal filters, and supplying the filtered air to an approved RPB loose fitting respirator head top.

Supplier: Thermo Fisher Scientific

En EVA. Pour plaques de scellage en PP et en PS.

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: RPB SAFETY

The RPB PX5 is a battery powered air purifying respirator fan unit which draws in contaminated air from the wearer's immediate vicinity, passing it through internal filters, and supplying the filtered air to an approved RPB loose fitting respirator head top.

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: U-Power

Made from EVA/textile.

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).

Supplier: U-Power

Dual PE/EVA support system with textile surface.

Supplier: EJENDALS

Insoles for medium arch support made from textile, soft EVA polyester based electro conductive thread and a TPU control bar.

Supplier: Bioss

FOXI1 is a member of the FOX family of transcription factors. The FOX family is a large group of proteins (consisting of at least 43 members) that share a common DNA binding domain termed winged-helix or forkhead domain. FOX transcription factors play important roles in development, differentiation, aging and hormone responsiveness. Localizing to the nucleus, FOXI1 functions as a transcription factor. Mice with mutated forms of FOXI1 show defects in ear development, implying that FOXI1 plays a significant role in the developmental pathway of ears and, in particular, the cochlea and vestibulum. FOXI1 is an upstream transcription regulator of Pendrin (a protein associated with deafness), suggesting a role for FOXI1 in the pathogenesis of Pendred syndrome (PS), a condition of nonsyndromic hearing loss and enlarged vestibular aqueduct (EVA).