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Proveedor: Apollo Scientific
Descripción: Methyl 1,2,3,4-tetra-O-acetyl-α-L-idopyranosyluronate ≥98%

Numero del catalogo: (BOSSBS-6852R-A750)
Proveedor: Bioss
Descripción: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction.
UOM: 1 * 100 µl


Proveedor: Thermo Fisher Scientific
Descripción: Ácido L-α-Aminoadípico 98%
Proveedor: Thermo Fisher Scientific
Descripción: L-Fenilalanina 98.5-101.0%, meets analytical specification of USP

FDS

Proveedor: TCI
Descripción: (±)-Ácido 5-(ditiolan-3-il)valerico ≥99.0% (by titrimetric analysis)

Numero del catalogo: (BOSSBS-15969R-A750)
Proveedor: Bioss
Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
UOM: 1 * 100 µl


Proveedor: Apollo Scientific
Descripción: Ethyl-2-chloro-2-(hydroxyimino)acetate 97%

Numero del catalogo: (TCIAN0014-25G)
Proveedor: TCI
Descripción: Disodium-2,7-naphthalenedisulphonate ≥98.0% (by titrimetric analysis)
UOM: 1 * 25 g


Proveedor: TCI
Descripción: N-Acetyl-DL-2-phenylglycine ≥98.0% (by HPLC, titration analysis)

Numero del catalogo: (APOSOR301370-1G)
Proveedor: Apollo Scientific
Descripción: 3-Amino-N-(tert-butoxycarbonyl)benzylamine 97%
UOM: 1 * 1 g


Numero del catalogo: (BOSSBS-15969R-CY5)
Proveedor: Bioss
Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-15969R-FITC)
Proveedor: Bioss
Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-6589R)
Proveedor: Bioss
Descripción: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
UOM: 1 * 100 µl


Numero del catalogo: (BOSSBS-12970R-A750)
Proveedor: Bioss
Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
UOM: 1 * 100 µl


Proveedor: TCI
Descripción: Ácido (R)-(+)-α-metoxi-α-(trifluorometil)fenilacetico ≥98.0% (by GC, titration analysis) optical resolving

Numero del catalogo: (TCIAB4281-5G)
Proveedor: TCI
Descripción: 1-Benzyl-N-carbobenzoxy-D-glutamate ≥98.0% (by HPLC, titration analysis)
UOM: 1 * 5 g


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El stock para este material es limitada pero puede estar disponible en un almacén cerca de usted. Por favor, asegúrese de que ha iniciado sesión en la web para que el stock disponible se puede mostrar. Si el call sigue apareciendo y usted necesita ayuda, por favor llámenos al 902 222 897 o por email en webshop.es@avantorsciences.com.
Este producto se trata de un artículo regulado sometido a normativa que restringe su venta. Si procede, nos pondremos en contacto con usted para solicitarle la licencia o declaración de uso necesaria para poder proceder al suministro del producto.
Este producto se trata de un artículo regulado sometido a normativa que restringe su venta.
Si procede, nos pondremos en contacto con usted para solicitarle la licencia o declaración de uso necesaria para poder proceder al suministro del producto.
Este producto ha sido bloqueado por su organización. Por favor, pónganse en contacto con su departamento de compras para obtener más información.
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