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Catalog Number: (97011-864)
Supplier: Sper Scientific
Description: The programmable refractometer is preloaded with the commonly used Brix (0–95%) and nD (refractive index) scales


Catalog Number: (89187-070)
Supplier: Atago
Description: In-line Refractometers designed for the measurement of refractive index, concentration and Brix scale.


Supplier: Wards
Description: Spectrometer prisms offer a different index of refraction for every need.

Catalog Number: (76545-890)
Supplier: Heathrow Scientific
Description: This digital honey refractometer has 4 scales. It measures brix, moisture, baume, and refractive index. These honey scales are used by beekeepers and in the food industry.


Catalog Number: (97011-862)
Supplier: Sper Scientific
Description: Measure concentrations in brix, salinity, refractive index, and clinical parameters with the full scale accuracy of 0.1% using CCD scanner (linear scanned array imaging) technology


Supplier: Atago
Description: Model PAL-RI is designed for measuring Refractive Index, the measurement will be displayed continuously like an electric newsboard once the sample has been placed

Catalog Number: (97011-858)
Supplier: Sper Scientific
Description: Measure concentrations in brix, salinity, refractive index, and clinical parameters with the full scale accuracy of 0.1% using CCD scanner (linear scanned array imaging) technology


Catalog Number: (76110-834)
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.


Catalog Number: (10491-884)
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.


Catalog Number: (75790-712)
Supplier: Prosci
Description: Alpha-Crystallin A Chain (CRYAA) belongs to the small heat shock protein (HSP20) family and can be induced by heat shock. The expression of CRYAA is preferentially restricted to the lens cell. CRYAA may contribute to the transparency and refractive index of the lens. CRYAA has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Two additional functions of CRYAA are an autokinase activity and participation in the intracellular architecture.


Catalog Number: (10491-888)
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.


Catalog Number: (10491-886)
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.


Catalog Number: (75788-926)
Supplier: Prosci
Description: alpha Crystallin B Chain (CRYAB) is a cytoplasmic protein that belongs to the small heat shock protein (HSP20) family. 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. Alpha crystallins acts as molecular chaperones and hold them in in large soluble aggregates. CRYAB is expressed widely in many tissues and organs. It may contribute to the transparency and refractive index of the lens. The deficiency of CRYAB is the cause of myopathy myofibrillar type 2 (MFM2) and cataract posterior polar type 2 (CTPP2).


Catalog Number: (10085-218)
Supplier: Proteintech
Description: Alpha B-crystallin, encoded by CRYAB gene, is multifunctional, serving as both a major structural protein in the lens and a small heat-shock protein in other tissues in mammals. Alpha B-crystallin may contribute to the transparency and refractive index of the lens. Single nucleotide polymorphisms (SNPs) in the promoter region of CRYAB gene have been associated with in multiple sclerosis. Mutations in the CRYAB gene cause distinct clinical phenotypes including isolated posterior polar cataract, myofibrillar myopathy, cardiomyopathy, or a multisystemic disorder combining all these features. Impairment of alpha-B crystallin dimerization may be relevant to the pathogenesis of these disorders.


Catalog Number: (76110-836)
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.


Supplier: MilliporeSigma
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.

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