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CRYBA2 monoclonal antibody (M04), clone 2G9

  • Catalog # : H00001412-M04
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  • Specification
  • Product Description:
  • Mouse monoclonal antibody raised against a partial recombinant CRYBA2.
  • Immunogen:
  • CRYBA2 (NP_005200.1, 94 a.a. ~ 193 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
  • Sequence:
  • SFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIR
  • Host:
  • Mouse
  • Reactivity:
  • Human
  • Isotype:
  • IgG2a Kappa
  • Quality Control Testing:
  • Antibody Reactive Against Recombinant Protein.
  • Storage Buffer:
  • In 1x PBS, pH 7.4
  • Storage Instruction:
  • Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.
  • Applications
  • Sandwich ELISA (Recombinant protein)
  • Sandwich ELISA (Recombinant protein)
  • Detection limit for recombinant GST tagged CRYBA2 is approximately 1ng/ml as a capture antibody.
  • PDF DownloadProtocol Download
  • ELISA
  • Application Image
  • Sandwich ELISA (Recombinant protein)
  • Sandwich ELISA (Recombinant protein)
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  • ELISA
  • Gene Information
  • Entrez GeneID:
  • 1412
  • Gene Name:
  • CRYBA2
  • Gene Alias:
  • -
  • Gene Description:
  • crystallin, beta A2
  • Gene Summary:
  • Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq
  • Other Designations:
  • eye lens structural protein
  • Related Disease
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