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Rabbit anti-Human CRYBB1 Polyclonal Antibody

The antibody against CRYBB1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-252 of human CRYBB1 (NP_001878.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.

ADA-04322A

The antibody against CRYBB1 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-252 of human CRYBB1 (NP_001878.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.

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Specifications


Cat.No ADA-04322A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCRYBB1
Target SynonymsCATCN3; CTRCT17; CRYBB1FormLiquid
Species ReactivityHuman, MouseIsotypeIgG
Storage Buffer50% Glycerol, PBS with 0.02% sodium azide, pH7.3.Purification MethodAffinity purification
Positive SamplesMouse eyeApplicationELISA, WB

Immunogen Information


Immunogen DescriptionRecombinant fusion protein containing a sequence corresponding to amino acids 1-252 of human CRYBB1 (NP_001878.1).Target SpeciesHuman
Uniprot IDP53674Immunogen Sequence
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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