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Rabbit anti-Human CRYBA4 Polyclonal Antibody

The antibody against CRYBA4 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-196 of human CRYBA4 (NP_001877.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.

ADA-05175A

The antibody against CRYBA4 was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 1-196 of human CRYBA4 (NP_001877.1) 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-05175A ClonalityPolyclonal
Host SpeciesRabbitTarget NameCRYBA4
Target SynonymsCYRBA4; CTRCT23; MCOPCT4; CRYBA4FormLiquid
Species ReactivityHumanIsotypeIgG
Storage Buffer50% Glycerol, PBS with 0.01% thimerosal, pH7.3.Purification MethodAffinity purification
Positive SamplesHeLa, 293TApplicationELISA, WB

Immunogen Information


Immunogen DescriptionRecombinant fusion protein containing a sequence corresponding to amino acids 1-196 of human CRYBA4 (NP_001877.1).Target SpeciesHuman
Immunogen SequenceMTLQCTKSAGPWKMVVWDEDGFQGRRHEFTAECPSVLELGFETVRSLKVLSGAWVGFEHAGFQGQQYILERGEYPSWDAWGGNTAYPAERLTSFRPAACANHRDSRLTIFEQENFLGKKGELSDDYPSLQAMGWEGNEVGSFHVHSGAWVCSQFPGYRGFQYVLECDHHSGDYKHFREWGSHAPTFQVQSIRRIQQUniprot IDP53673
Background Information
  • Uniprot Id

    P53673

  • Target Species

    Human

  • Target Name

    CRYBA4

  • Target Full Name

    Beta-crystallin A4

  • Target Function

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

  • Target Involvement

    Cataract 23, multiple types (CTRCT23)

  • Target Protein Families

    Beta/gamma-crystallin family

  • Target Synonyms

    Beta A4 crystallin; Beta crystallin A4; Beta-A4 crystallin; Beta-crystallin A4; CRBA4_HUMAN; CRYBA4; Crystallin beta A4; Crystallin; beta polypeptide A4; CTRCT23; Eye lens structural protein; MCOPCT4

  • 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, is part of a gene cluster with beta-B1, beta-B2, and beta-B3.

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