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Supplier: VWR Collection
Description: Experience the next level of high-performance liquid chromatography with the Chromaster Plus HPLC system. This latest version boasts a sleek new design and enhanced performance features, including the upgraded CM5310 column oven and CM5410 UV detector. The new design offers a modern and user-friendly interface, while the enhanced performance of the CM5310 column oven and CM5410 UV detector ensures superior results. Additionally, users can enjoy peace of mind with an extended warranty coverage.

Supplier: Apollo Scientific
Description: Affords low refractive index polymer.

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Supplier: VWR Collection
Description: Dual-scale handheld refractometers designed to provide ranges of Brix (sugar concentration) and refractive index measurements.

Supplier: Merck
Description: Canada balsam is a commonly used mounting medium to prepare permanent slides for microscopy. It is produced from the resin of the balsam fir tree and its use can be combined with xylene-containing specimens. (Refractive index (20°C) 1.515 - 1.530) Canada balsam is an IVD product and CE registered.
Catalog Number: (C9368-30ML)
Supplier: SIGMA ALDRICH MICROSCOPY
Description: CC/mount is an aqueous based permanent mounting medium with a very high refractive index, which when applied to the stained tissue sections can store the tissue specimens permanently without the fading of the chromogens. Because of the superior refractive index of CC/mount, tissues mounted in this medium look like specimens mounted with organic based mounting media. No coverslipping is required with CC/mount. However, if coverslipping is required, dried CC/mount can be post mounted by using an organic based mounting medium. CC/mount permits the long-term storage of antigens localised using organic insoluble chromogen substrates, including AEC, DAB, Fast Red, BCIP/NBT, BCIP/INT and fluorescent dyes like FITC and phycobiliproteins. The high pH of CC/mount ensures increased stability of fluorescence intensity.
UOM: 1 * 30 mL


Supplier: cphnano
Description: Get accurate quantification by upgrading a UV-Vis spectrophotometer with user-friendly cuvettes. The NanoCuvette™ One expands the capabilities of an UV/Vis spectrophotometer to include quantification via refractive index for QC, kinetics, and 0,5 μl sample measurements.

Catalog Number: (635-0480)
Supplier: BELLINGHAM STANLEY
Description: The Abbe refractometer is designed for applications in educational establishments and laboratories, where wide refractive index ranges are required, or where sample throughput is relatively low.
UOM: 1 * 1 items


Catalog Number: (BOSSBS-9585R-CY3)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-9585R-A488)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-9585R-A750)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated and 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. S-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. S-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. S-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13276R-A680)
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 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


Catalog Number: (BOSSBS-13276R-A350)
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 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


Catalog Number: (BOSSBS-13276R-FITC)
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 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


Catalog Number: (BOSSBS-9585R-CY5.5)
Supplier: Bioss
Description: 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


Catalog Number: (BOSSBS-13276R-HRP)
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 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


Catalog Number: (BOSSBS-13276R-A647)
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 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


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organisation. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
Product(s) marked with this symbol are discontinued - sold till end of stock. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service on +353 1 8822222.
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