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Imagem do Produto-111-1593

Safety spectacles, SecureFit™ 200

Descrição: Stylish, lightweight designed safety glasses features proprietary 3M™ Pressure Diffusion Temple Technology that helps diffuse pressure over the ear to enhance frame comfort while not compromising the security of fit across a diverse workforce.
Código de Artigo: 111-1593
UOM: 1 * 1 unid.
Fornecedor: 3M
Image Unavailable-BOSSBS-12463R-A750

Anti-alpha B Crystallin Ser59 Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Descrição: 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. Since 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 30-40 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.
Código de Artigo: BOSSBS-12463R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-15969R-CY5

Anti-alpha B Crystallin Ser19 Rabbit Polyclonal Antibody (Cy5)

Descrição: 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.
Código de Artigo: BOSSBS-15969R-CY5
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-15969R-FITC

Anti-alpha B Crystallin Ser19 Rabbit Polyclonal Antibody (FITC)

Descrição: 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.
Código de Artigo: BOSSBS-15969R-FITC
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-4651R-A750

Anti-Alpha B Crystallin Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Descrição: 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. Since lens central fibre 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 30-40 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.
Código de Artigo: BOSSBS-4651R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-12970R-A350

Anti-CRYAB Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Descrição: 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. Since 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 30-40 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. [provided by RefSeq, Jul 2008].
Código de Artigo: BOSSBS-12970R-A350
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-12970R-A647

Anti-CRYAB Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Descrição: 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. Since 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 30-40 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. [provided by RefSeq, Jul 2008].
Código de Artigo: BOSSBS-12970R-A647
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-12963R-CY3

Anti-CRYAB Rabbit Polyclonal Antibody (Cy3®)

Descrição: 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. Since 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 30-40 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. [provided by RefSeq, Jul 2008].
Código de Artigo: BOSSBS-12963R-CY3
UOM: 1 * 100 µl
Fornecedor: Bioss
Image Unavailable-BOSSBS-4651R-A647

Anti-CRYAB Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Descrição: 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. Since 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 30-40 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. [provided by RefSeq, Jul 2008].
Código de Artigo: BOSSBS-4651R-A647
UOM: 1 * 100 µl
Fornecedor: Bioss
Imagem do Produto-JSPA1EIGGREEN23SKN

Safety spectacles, Eiger™

Descrição: Sporty design with optimal curved lens and large field of vision.
Código de Artigo: JSPA1EIGGREEN23SKN
UOM: 1 * 1 unid.
Fornecedor: JSP
Imagem do Produto-111-2577

Safety prescription spectacles, Solus™ 2000 series

Descrição: Comfortable, stylish eyewear with a vast array of colour and lens tint options, the Solus™ 2000 prescription series provides eye protection with a stylish flare.
Código de Artigo: 111-2577
UOM: 1 * 1 unid.
Fornecedor: 3M
Image Unavailable-BOSSBS-13276R-A750

Anti-gamma Crystallin Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Descrição: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. gamma-crystallins are structural proteins in the lens, and they exists as monomers which typically lack connecting peptides and terminal extensions. The gamma-crystallins include seven closely related gamma A, gamma B, gamma C, gamma D, gamma E, gamma F, and gamma G-crystallin, as well as the gamma N and gamma S-crystallin genes. The gamma-crystallins are differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.
Código de Artigo: BOSSBS-13276R-A750
UOM: 1 * 100 µl
Fornecedor: Bioss
Imagem do Produto-MMMASF203AFP

SecureFit™ 200 Safety Glasses

Descrição: 3M™ SecureFit™ 200 series are lightweight safety glasses with 3M™ Pressure Diffusion Temple Technology. The glasses feature a wraparound design that’s secure and comfortable. They are available in various lens tints.
Código de Artigo: MMMASF203AFP
UOM: 1 * 1 unid.
Fornecedor: 3M
Imagem do Produto-630-8327

Linen testers

Descrição: Satin matt chrome plated brass frame with silicate glass lens.
Código de Artigo: 630-8327
UOM: 1 * 1 unid.
Fornecedor: ESCHENBACH OPTIK
Imagem do Produto-SYNOGBOX-F3-LFB

Gel documentation system, Syngene G:BOX-F³

Descrição: The Syngene G:BOX-F³ gel imaging system is designed for general fluorescence applications, including DNA and protein analysis. The range of applications available can be extended by adding lighting modules*. Driven from a database containing hundreds of application protocols, functional control of the G:BOX-F³ is handled by the GeneSys automatic control software, although full manual control is also possible. It has a 3,8 megapixel camera with motorised (f/1,2) lens , which gives high quality images with undetectable noise.
Código de Artigo: SYNOGBOX-F3-LFB
UOM: 1 * 1 unid.
Fornecedor: Syngene (a division of the Synoptics group)
Image Unavailable-BOSSBS-11015R-CY5

Anti-RPSA Rabbit Polyclonal Antibody (Cy5®)

Descrição: Phakinin is a membrane-associated and cytoskeletal intermediate filament (IF) protein specific to the eye lens. IFs are cytoskeletal structures that typically contain a head, rod and tail domain. Unlike most IFs, Phakinin completely lacks the C-terminal tail domain thus contributing to the unique structure of the beaded filament that is specific to the lens. Phakinin is required for the assembly of beaded filaments and cytoskeletal networks that are important for the long-term maintenance of optical properties and transparency of the lens. Phakinin copolymerizes with Filensin, another IF protein, to form the 10-nm filamentous structures of the beaded filaments. Phakinin is also capable of self-assembling into filament-like structures that form thicker bundles. Mutations in the gene encoding Phakinin can result in lens cataract.
Código de Artigo: BOSSBS-11015R-CY5
UOM: 1 * 100 µl
Fornecedor: Bioss
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