beta Crystallin A3 (CRYBA1) (NM_005208) Human Mass Spec Standard

CAT#: PH321965

CRYBA1 MS Standard C13 and N15-labeled recombinant protein (NP_005199)

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

• Tag: C-Myc/DDK
• Species: Human
• Expression Host: HEK293
• Expression cDNA Clone or AA Sequence: RC221965
• Predicted MW: 25.1 kDa
• Protein Sequence:
  Sequence Link

  >RC221965 protein sequence
  Red=Cloning site Green=Tags(s)
  
  METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVES
  GAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKMTIFEKENFIGRQWE
  ISDDYPSLQAMGWFNNEVGSMKIQSGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGSHAQTSQIQSI
  RRIQQ
  
  TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Concentration: 50 ug/ml as determined by BCA
• Labeling Method: Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine
• Buffer: 100 mM glycine, 25 mM Tris-HCl, pH 7.3. Store at -80°C. Avoid repeated freeze-thaw cycles. Stable for 3 months from receipt of products under proper storage and handling conditions.

Reference Data

• RefSeq: NP_005199
• RefSeq Size: 806
• RefSeq ORF: 645
• Synonyms: CRYB1; CTRCT10
• Locus ID: 1411
• UniProt ID: P05813
• Cytogenetics: 17q11.2
• 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]'