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

CAT#: PH321965

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



  View other "beta Crystallin A3" proteins (3)

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CNY 19,520.00


货期*
4周

规格
    • 10 ug

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经常一起买 (2)
Transient overexpression lysate of crystallin, beta A1 (CRYBA1)
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Specifications

Product Data
Description CRYBA1 MS Standard C13 and N15-labeled recombinant protein (NP_005199)
Species Human
Expression Host HEK293
Expression cDNA Clone or AA Sequence RC221965
Predicted MW 25.1 kDa
Protein Sequence
Tag C-Myc/DDK
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
Reference Data
RefSeq NP_005199
RefSeq Size 806
RefSeq ORF 645
Synonyms CRYB1; CTRCT10
Locus ID 1411
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]
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