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Katalogové číslo: (BOSSBS-13695R-HRP)
Dodavatel: Bioss
Popis: The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (PRSIXW-7061)
Dodavatel: ProSci Inc.
Popis: Human complement component C3. Complement C3 contains two chains linked by a disulfide bond. Its activation by a C3 convertase releases the C3a anaphylatoxin from the amino end of the beta chain and generates C3b, which associates with the Bb fragment of complement factor B to form the alternative-complement-pathway C3/C5 convertase.C3a anaphylatoxin is a vasoactive peptide and a mediator of inflammation. C3b, with its highly reactive thiol group, binds to the surface of foreign particles and facilitates phagocytosis. It binds to complement C5 and renders it susceptible to proteolysis by the classical-complement-pathway C3/C5 convertase. The activity of C3b is regulated by proteolytic cleavage involving factors H and I. Its degradation products can also be biologically active.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (786-180)
Dodavatel: G-Biosciences
Popis: Mammalian Cell PE LB™ has been developed for extraction of total biologically active, soluble proteins from mammalian cultured cells. The Mammalian Cell PE LB™ is based on organic buffering agents and utilises a mild non-ionic detergent, chelating agent, and a proprietary combination of various salts and agents to enhance extraction and stability of proteins. Depending on the required downstream application, additional agents such as reducing agents, phosphatase and protease inhibitors may be added into Mammalian Cell PE LB™. Mammalian Cell PE LB™ has been tested on a wide variety of mammalian cells and can be used for both suspension and adherent cells.
Měrná jednotka: 1 * 500 mL


Katalogové číslo: (BOSSBS-11080R-A680)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (PRSI92-686)
Dodavatel: ProSci Inc.
Popis: Platelet-derived growth factor receptors (PDGFR) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family. The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. PDGFs bind to the protein tyrosine kinase receptors PDGF receptor- alpha and - beta . These two receptor isoforms dimerise upon binding the PDGF dimer, leading to three possible receptor combinations, namely - alpha alpha, - beta beta and - alpha beta . PDGFR alpha and PDGFR beta are members of the class III RTK family. Inappropriate PDGFR alpha and PDGFR beta signalling has been linked to a number of proliferative disorders.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (ICNA11TWEEN201)
Dodavatel: MP Biomedicals
Popis: TWEEN 20 is a nonionic detergent widely used in biochemical applications, such as emulsifying agents for the preparation of stable oil-inwater emulsions. It has been used in preextraction of membranes to remove peripheral proteins. TWEEN 20 has been used as a blocking agent for membrane based immunoassays at a typical concentration of 0.05%. TWEEN 20 can be used for lysing mammalian cells at a concentration of 0.05 to 0.5%.

TWEEN 20 is a polyoxyethylene sorbitol ester.

Typical Working Concentration:
Extraction of membrane-bound proteins: 2%; blocking agent for membrane based immunoassays at a typical concentration of 0.05%; lysing mammalian cells at a concentration of 0.05 to 0.5%.
Měrná jednotka: 1 * 500 mL


Katalogové číslo: (PRSI92-701)
Dodavatel: ProSci Inc.
Popis: Platelet-derived growth factor receptors (PDGFR) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family. The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. PDGFs bind to the protein tyrosine kinase receptors PDGF receptor- alpha and - beta . These two receptor isoforms dimerise upon binding the PDGF dimer, leading to three possible receptor combinations, namely - alpha alpha, - beta beta and - alpha beta . PDGFR alpha and PDGFR beta are members of the class III RTK family. Inappropriate PDGFR alpha and PDGFR beta signalling has been linked to a number of proliferative disorders.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (BOSSBS-11080R-FITC)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-CY7)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-CY3)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-A555)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-A350)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-A750)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-CY5)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-HRP)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11080R-A647)
Dodavatel: Bioss
Popis: 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].
Měrná jednotka: 1 * 100 µl


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