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Image Unavailable-ESCH1624511

MaxDetail® Maginifying Spectacles (for near) - Dark Grey

Código de Artigo: (ESCH1624511)
Fornecedor: ESCHENBACH OPTIK
Descrição: These hands-free, head-mounted glasses provide 2X magnification and can be adjusted so that each eye lens can be focused separately [±3 diopters], making the system adaptable to most patients. The glasses will focus on near objects with working distances of 25,4 mm and are perfect for any near viewing activity where a magnified image is helpful.
UOM: 1 * 1 unid.
Imagem do Produto-111-1841

VWR®, Óculos, Kingston

Código de Artigo: (111-1841)
Fornecedor: VWR Collection
Descrição: Wrap-around modern style goggles, especially designed for small faces, provides excellent panoramic vision. The goggles consist of a PC lens, PVC frame and polyester/rubber headband.
UOM: 1 * 1 unid.
Imagem do Produto-1.09512.0003

Papel de amido com iodeto de potássio Reag.Ph.Eur., Supelco®

Código de Artigo: (1.09512.0003)
Fornecedor: Merck
Descrição: Potassium iodine paper is used for the determination of oxidising agents.
UOM: 1 * 3 Rolo

MSDS Certificados


Image Unavailable-BOSSBS-15969R-A488

Anti-alpha B Crystallin Ser19 Rabbit Polyclonal Antibody (ALEXA FLUOR® 488)

Código de Artigo: (BOSSBS-15969R-A488)
Fornecedor: Bioss
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.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-15969R-A647

Anti-alpha B Crystallin Ser19 Rabbit Polyclonal Antibody (ALEXA FLUOR® 647)

Código de Artigo: (BOSSBS-15969R-A647)
Fornecedor: Bioss
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.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-4651R-FITC

Anti-CRYAB Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Código de Artigo: (BOSSBS-4651R-FITC)
Fornecedor: Bioss
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].
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-4651R-A488

Anti-CRYAB Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Código de Artigo: (BOSSBS-4651R-A488)
Fornecedor: Bioss
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].
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-2506R-HRP

Anti-AQP7 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Código de Artigo: (BOSSBS-2506R-HRP)
Fornecedor: Bioss
Descrição: Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein "aquaporin". Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues. AQP0 or MIP26 (major intrinsic protein 26kD), and Aquaporin 1 (AQP1, purified from red cells) also called CHIP28 (channel forming integral protein, 28kD; 268aa; gene locus 7p14) has been the foundation of the growing family of aquaporin. The lens specific AQP0 represents up to 80% of total lens membrane protein. Defects in MIP26 are cause of autosomal dominant cataract. The cataract Fraser mutation (CATFR or Shriveled) is a transposon induced splicing error that substitutes a long terminal repeat sequence for the C terminus of MIP. The lens opacity mutation (LOP) is an amino acid substitution that inhibits targeting of MIP to the cell membrane.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9585R-A488

Anti-CRYGS Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Código de Artigo: (BOSSBS-9585R-A488)
Fornecedor: Bioss
Descrição: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl
Imagem do Produto-MMMASCCS07SGAF-GRN

Solus™ CCS Safety Glass, Scotchgard™ Anti-Fog/Anti-Scratch Coating

Código de Artigo: (MMMASCCS07SGAF-GRN)
Fornecedor: 3M
Descrição: 3M™ Solus™ CCS Safety Glasses are rimless safety glasses that feature lime green temples with a Corded Control System (CCS) for attaching corded earplugs. The polycarbonate lens features a Scotchgard™ anti-fog and anti-scratch coating on both sides for increased durability and improved vision.
UOM: 1 * 1 unid.
Image Unavailable-BOSSBS-2506R-CY7

Anti-AQP7 Rabbit Polyclonal Antibody (Cy7®)

Código de Artigo: (BOSSBS-2506R-CY7)
Fornecedor: Bioss
Descrição: Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein "aquaporin". Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues. AQP0 or MIP26 (major intrinsic protein 26kD), and Aquaporin 1 (AQP1, purified from red cells) also called CHIP28 (channel forming integral protein, 28kD; 268aa; gene locus 7p14) has been the foundation of the growing family of aquaporin. The lens specific AQP0 represents up to 80% of total lens membrane protein. Defects in MIP26 are cause of autosomal dominant cataract. The cataract Fraser mutation (CATFR or Shriveled) is a transposon induced splicing error that substitutes a long terminal repeat sequence for the C terminus of MIP. The lens opacity mutation (LOP) is an amino acid substitution that inhibits targeting of MIP to the cell membrane.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-13276R-A488

Anti-CRYG Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Código de Artigo: (BOSSBS-13276R-A488)
Fornecedor: Bioss
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.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-12859R

Anti-CRYBA1 Rabbit Polyclonal Antibody

Código de Artigo: (BOSSBS-12859R)
Fornecedor: Bioss
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 a, b, and g families, and the b- and g-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. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9585R-A647

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

Código de Artigo: (BOSSBS-9585R-A647)
Fornecedor: Bioss
Descrição: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9585R-CY5.5

Anti-CRYGS Rabbit Polyclonal Antibody (Cy5.5®)

Código de Artigo: (BOSSBS-9585R-CY5.5)
Fornecedor: Bioss
Descrição: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl
Imagem do Produto-MMMAETUI6

Bolsa para óculos

Código de Artigo: (MMMAETUI6)
Fornecedor: 3M
Descrição: Black microfibre pouch for standard glasses and spectacles.
UOM: 1 * 1 unid.
Preço sob consulta
O stock para este item é limitado. Por favor, certifique-se de que efetuou o seu login para visualizar o stock disponível. Se a call ainda é exibida e precisar de ajuda, por favor, ligue para 213 600 770
O stock para este item é limitado. Por favor, certifique-se de que efetuou o seu login para visualizar o stock disponível. Se a call está visível e precisar de ajuda, por favor, ligue para 213 600 770
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão.
Este produto está bloqueado. Para obter mais informações, contacte a VWR através do número 213 600 770.
O produto pretendido já não se encontra disponível. O produto indicado é um substituto.
Este produto encontra-se em rutura de stock. Poderá encontrar alternativas pesquisando pelo código de artigo indicado acima. Se precisar de ajuda, por favor contacte a VWR através do 213 600 770.
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