Natural Cow alpha A Crystallin protein (ab113181)

Overview

Description

  • NatureNatural
  • SourceNative
  • Amino Acid Sequence
    • AccessionP02470
    • SpeciesCow
    • Molecular weight20 kDa
    • Amino acids1 to 172
    • Additional sequence informationSource = bovine eye lens

Associated products

Specifications

Our Abpromise guarantee covers the use of ab113181 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

  • Purity>= 80 % SDS-PAGE.
    Purified by multi-step chromatography.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.20
    Constituents: 98% PBS, 0.88% Sodium chloride, 0.69% Phosphate Buffer

General Info

  • Alternative names
    • Acry 1
    • Alpha crystallin A chain
    • Alpha-crystallin A chain
    • CRYA 1
    • CRYA1
    • CRYAA
    • CRYAA_HUMAN
    • Crystallin alpha 1
    • Crystallin alpha A
    • Heat shock protein beta 4
    • Heat shock protein beta-4
    • HSPB 4
    • HspB4
    • short form
    • Zonular Central Nuclear Cataract
    see all
  • FunctionMay contribute to the transparency and refractive index of the lens.
  • Involvement in diseaseDefects in CRYAA are a cause of cataract autosomal dominant (ADC) [MIM:604219]. Cataract is an opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Cataract is the most common treatable cause of visual disability in childhood.
  • Sequence similaritiesBelongs to the small heat shock protein (HSP20) family.
  • Post-translational
    modifications
    O-glycosylated; contains N-acetylglucosamine side chains.
    Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.
    Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual.
  • Cellular localizationCytoplasm. Nucleus. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
  • Information by UniProt

References for Natural Cow alpha A Crystallin protein (ab113181)

ab113181 has not yet been referenced specifically in any publications.

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