APPLICATION
PROPERTIES
Form
Liquid
Buffer
20mM Tris-HCl, 100mM NaCl, 20% Glycerol, 1mM DTT
Preservative
No preservative
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1 mg/ml (Please refer to the vial label for the specific concentration.)
Region/Sequence
Full length protein, N-terminal His-Tag; MGSSHHHHHH SSGLVPRGSH MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ
Expression System
E. coli
Purity
> 95% by SDS-PAGE.
Conjugation
Unconjugated
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
TARGET
Synonyms
crystallin beta A4 , CTRCT23 , CYRBA4 , MCOPCT4
Background
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, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]
Database
Research Area
DATA IMAGES
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GTX67322-pro Image
3μg Human beta A4 Crystallin protein (GTX67322-pro) by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
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REFERENCE
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REVIEW
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