You Searched For: Lens+Papers

Catalog Number: (BOSSBS-15969R-FITC)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-4651R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12970R-A647)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-12970R-A350)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-4651R-A647)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-12963R-CY3)

Supplier: Bioss

Description: 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

Supplier: SCHOTT AG Lighting and imaging

Description: Focusing lens for light guides without filter, For: Cold light source KL 200/300 LED

Catalog Number: (BOSSBS-11015R-FITC)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Supplier: 3M

Description: 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.

Catalog Number: (BOSSBS-12859R-A488)

Supplier: Bioss

Description: 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

Catalog Number: (BOSSBS-12859R-A555)

Supplier: Bioss

Description: 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

Catalog Number: (87806.600)

Supplier: VWR Chemicals

Description: Supplied with certificate of analysis. Normally manufactured to order. Please check with customer services.

UOM: 1 * 50 Tests

Certificates

Catalog Number: (BOSSBS-13200R)

Supplier: Bioss

Description: This intronless gene belongs to the forkhead family of transcription factors, which is characterized by a distinct forkhead domain. The protein encoded functions as a lens-specific transcription factor and plays an important role in vertebrate lens formation. Mutations in this gene are associated with anterior segment mesenchymal dysgenesis and congenital primary aphakia. [provided by RefSeq, Dec 2009].

UOM: 1 * 100 µl

Catalog Number: (ESCH1511003)

Supplier: ESCHENBACH OPTIK

Description: High quality stand for the mobilux® LED that can be used in the flat position for tremble-free reading and viewing, as well as in an upright position to free hands for carrying out work behind the lens.

UOM: 1 * 1 items

Catalog Number: (BOSSBS-11015R-A488)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11015R-A647)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl