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Rabbit anti-Human CRYBB1 Polyclonal Antibody

The antibody against CRYBB1 was raised in rabbit using the Human CRYBB1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.

ADC-48852A

The antibody against CRYBB1 was raised in rabbit using the Human CRYBB1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB.

$600.00

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Specifications


Cat.No ADC-48852A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCRYBB1
FormLiquidSpecies ReactivityHuman, Mouse, Rat
IsotypeIgGStorage Buffer50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.02% sodium azide
Purification MethodAntigen affinity purifiedConjugateNon-conjugated
ApplicationELISA, WBStorageUpon receipt

Immunogen Information


Immunogen DescriptionHuman CRYBB1Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP53674
Background Information
  • Uniprot Id

    P53674

  • Target Species

    Human

  • Target Name

    CRYBB1

  • Target Full Name

    Beta-crystallin B1

  • Target Function

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

  • Target Involvement

    Cataract 17, multiple types (CTRCT17)

  • Target Protein Families

    Beta/gamma-crystallin family

  • Target Synonyms

    Beta crystallin B1; Beta-B1 crystallin; Beta-crystallin B1; CATCN3; CRBB1_HUMAN; CRYBB 1; Crybb1; Crystallin beta B1; CTRCT17; Eye lens structural protein; OTTHUMP00000028719

  • 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 basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3.

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