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CRYBB1 (Human) Recombinant Protein (P01)

  • Catalog # : H00001414-P01
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  • Specification
  • Product Description:
  • Human CRYBB1 full-length ORF ( AAH36790.1, 1 a.a. - 252 a.a.) recombinant protein with GST-tag at N-terminal.
  • Sequence:
  • Host:
  • Wheat Germ (in vitro)
  • Theoretical MW (kDa):
  • 53.46
  • Purification:
  • Glutathione Sepharose 4 Fast Flow
  • Quality Control Testing:
  • 12.5% SDS-PAGE Stained with Coomassie Blue.

    QC Testing of H00001414-P01
  • Storage Buffer:
  • 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer.
  • Storage Instruction:
  • Store at -80°C. Aliquot to avoid repeated freezing and thawing.
  • Note:
  • Best use within three months from the date of receipt of this protein.
  • Applications
  • Enzyme-linked Immunoabsorbent Assay
  • Western Blot (Recombinant protein)
  • Antibody Production
  • Protein Array
  • Application Image
  • Enzyme-linked Immunoabsorbent Assay
  • Western Blot (Recombinant protein)
  • Antibody Production
  • Protein Array
  • Gene Information
  • Entrez GeneID:
  • 1414
  • Gene Name:
  • CRYBB1
  • Gene Alias:
  • CATCN3
  • Gene Description:
  • crystallin, beta B1
  • Gene Summary:
  • 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. [provided by RefSeq
  • Other Designations:
  • OTTHUMP00000028719,eye lens structural protein
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