Recombinant Human alpha A Crystallin protein (ab113189)



  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP02489
    • SpeciesHuman
    • Molecular weight20 kDa including tags
    • Amino acids1 to 173
    • TagsHis tag N-Terminus


Our Abpromise guarantee covers the use of ab113189 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> 95 % SDS-PAGE.
    ab11318 is 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: 7.50
    Constituents: 0.61% Tris, 0.08% DTT, 0.29% Sodium chloride

General Info

  • Alternative names
    • Acry 1
    • Alpha crystallin A chain
    • Alpha-crystallin A chain
    • CRYA 1
    • CRYA1
    • CRYAA
    • 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
    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

Recombinant Human alpha A Crystallin protein images

  • SDS-PAGE showing ab113189
    Lane 1: 0.5µg protein
    Lane 2: 1.0µg protein
    Lane 3: 2.0µg protein
    Lane 4: 4.0µg protein
  • All lanes : anti-alpha A Crystallin pAb

    Lane 1 : Recombinant Human alpha A Crystallin protein (ab113189) at 0.1 µg
    Lane 2 : Recombinant Human alpha A Crystallin protein (ab113189) at 0.2 µg
    Lane 3 : Native Cow alpha A Crystallin protein

References for Recombinant Human alpha A Crystallin protein (ab113189)

ab113189 has not yet been referenced specifically in any publications.

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