CRYBA2 (NM_005209) Human Mass Spec Standard

SKU PH316085

CRYBA2 MS Standard C13 and N15-labeled recombinant protein (NP_005200)

Product Data

• Tag: C-Myc/DDK
• Species: Human
• Expression Host: HEK293
• Expression cDNA Clone or AA Sequence: [RC216085]
• Predicted MW: 22.1 kDa
• Protein Sequence:
  Protein Sequence

  >RC216085 protein sequence; Red=Cloning site Green=Tags(s); ; MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFIL; EKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDV; GSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH; ; TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Labeling Method: Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3
• Storage: Store at -80°C. Avoid repeated freeze-thaw cycles.
• Stability: Stable for 3 months from receipt of products under proper storage and handling conditions.
• Shipping: Dry Ice

Reference Data

• RefSeq: NP_005200
• RefSeq Size: 709
• RefSeq ORF: 591
• Synonyms: crystallin, beta A2; eye lens structural protein
• Locus ID: 1412
• UniProt ID: P53672
• Cytogenetics: 2q35
• 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, Jul 2008]