CRYBB3 (NM_004076) Human Recombinant Protein

SKU TP316611M

Recombinant protein of human crystallin, beta B3 (CRYBB3), 100 µg

Product Data

• Species: Human
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  >RC216611 protein sequence; Red=Cloning site Green=Tags(s); ; MAEQHGAPEQAAAGKSHGDLGGSYKVILYELENFQGKRCELSAECPSLTDSLLEKVGSIQVESGPWLAFE; SRAFRGEQFVLEKGDYPRWDAWSNSRDSDSLLSLQPLNIDSPDHKLHLFENPAFSGRKMEIVDDDVPSLW; AHGFQDRVASVRAINGTWVGYEFPGYRGRQYVFERGEYRHWNEWDASQPQLQSVRRIRDQKWHKRGRFPS; S; ; TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Tag: C-Myc/DDK
• Predicted MW: 24.1 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
• Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Shipping: Dry Ice

Reference Data

• RefSeq: NP_004067
• Locus ID: 1417
• UniProt ID: P26998
• Cytogenetics: 22q11.23
• RefSeq Size: 896
• RefSeq ORF: 633
• Synonyms: CATCN2; CRYB3; CTRCT22
• 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, is part of a gene cluster with beta-A4, beta-B1, and beta-B2. Mutations in this gene result in cataract congenital nuclear autosomal recessive type 2. [provided by RefSeq, Feb 2013]