Recombinant Human beta Crystallin A3 protein (ab116990)

Overview

Description

  • NatureRecombinant
  • SourceWheat germ
  • Amino Acid Sequence
    • AccessionP05813
    • SpeciesHuman
    • Molecular weight37 kDa including tags
    • Amino acids116 to 215

Specifications

Our Abpromise guarantee covers the use of ab116990 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

    ELISA

    SDS-PAGE

  • FormLiquid
  • Additional notesProtein concentration is above or equal to 0.05 mg/ml.
    This protein is best used within three months from the date of receipt.
  • 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: 8.00
    Constituents: 0.79% Tris HCl, 0.3% Glutathione

General Info

  • Alternative names
    • Beta crystallin A3
    • Beta crystallin A3 isoform A1 Delta4 form
    • Beta crystallin A3 isoform A1 Delta7 form
    • Beta crystallin A3 isoform A1 Delta8 form
    • Beta-crystallin A3
    • CRBA1_HUMAN
    • CRYB1
    • CRYBA1
    • Crystallin beta A1
    • Crystallin beta A3
    • Delta8 form
    • Eye lens structural protein
    • isoform A1
    see all
  • FunctionCrystallins are the dominant structural components of the vertebrate eye lens.
  • Involvement in diseaseDefects in CRYBA1 are the cause of cataract congenital zonular with sutural opacities (CCZS) [MIM:600881]. A form of zonular cataract. Zonular or lamellar cataracts are concentric opacities, broad or narrow, usually consisting of powdery white dots affecting one lamella or zonule of an otherwise clear lens.
  • Sequence similaritiesBelongs to the beta/gamma-crystallin family.
    Contains 4 beta/gamma crystallin 'Greek key' domains.
  • DomainHas a two-domain beta-structure, folded into four very similar Greek key motifs.
  • Post-translational
    modifications
    Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.
    S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.
    Isoform A1 initiator methionine is removed. The new N-terminal amino acid is then N-acetylated.
  • Information by UniProt

Recombinant Human beta Crystallin A3 protein images

  • 12.5% SDS-PAGE showing ab116990 at approximately 36.63kDa.
    Stained with Coomassie Blue.

References for Recombinant Human beta Crystallin A3 protein (ab116990)

ab116990 has not yet been referenced specifically in any publications.

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