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Rabbit anti-Human CRYBA1 Polyclonal Antibody

The antibody against CRYBA1 was raised in rabbit using the Recombinant Human Beta-crystallin A3 protein (1-215AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC, IF.

ADC-22152A

The antibody against CRYBA1 was raised in rabbit using the Recombinant Human Beta-crystallin A3 protein (1-215AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC, IF.

$299.00

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Specifications


Cat.No ADC-22152A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCRYBA1
FormLiquidSpecies ReactivityHuman, Mouse
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISA, IF, IHC, WBStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Beta-crystallin A3 protein (1-215AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP05813
Background Information
  • Uniprot Id

    P05813

  • Target Species

    Human

  • Target Name

    CRYBA1

  • Target Full Name

    Beta-crystallin A3

  • Target Function

    Crystallins are the dominant structural components of the vertebrate eye lens.

  • Target Involvement

    Cataract 10, multiple types (CTRCT10)

  • Target Protein Families

    Beta/gamma-crystallin family

  • Target Synonyms

    Beta crystallin A3 isoform A1 Delta4 form; Beta crystallin A3; 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

  • Target Background

    Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.

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