beta Crystallin A3 (CRYBA1) (NM_005208) Human Recombinant Protein

CAT#: TP321965

Recombinant protein of human crystallin, beta A1 (CRYBA1)

Product Images

Coomassie blue staining of purified CRYBA1 protein (Cat# TP321965). The protein was produced from HEK293T cells transfected with CRYBA1 cDNA clone (Cat# RC221965) using MegaTran 2.0 (Cat# TT210002).

Specifications

Product Data

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

  Recombinant protein was produced with TrueORF clone, RC221965. Click on the TrueORF clone link to view cDNA and protein sequences.
• Tag: C-Myc/DDK
• Predicted MW: 25 kDa
• Concentration: >50 ug/mL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol
• Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
• 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.

Reference Data

• RefSeq: NP_005199
• Locus ID: 1411
• UniProt ID: P05813
• Cytogenetics: 17q11.2
• Refseq Size: 806
• Refseq ORF: 645
• Synonyms: CRYB1; CTRCT10
• 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 acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'. [provided by RefSeq, Jul 2008]'