Beta-crystallin A4 (1-196, His-tag) Human Protein
CAT#: AR39107PU-N
Beta-crystallin A4 (1-196, His-tag) human recombinant protein, 0.1 mg
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CNY 8,900.00
货期*
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规格
Specifications
Product Data | |
Species | Human |
Expression Host | E. coli |
Expression cDNA Clone or AA Sequence |
MGSSHHHHHH SSGLVPRGSH MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ
|
Tag | His-tag |
Predicted MW | 24.5 kDa |
Concentration | lot specific |
Purity | >95% |
Buffer | Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.1M NaCl, 1 mM DTT |
Preparation | Liquid purified protein |
Protein Description | Recombinant human CRYBA4 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
Storage | Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer. Avoid repeated freezing and thawing. |
Stability | Shelf life: one year from despatch. |
Reference Data | |
RefSeq | NP_001877 |
Locus ID | 1413 |
UniProt ID | P53673, A0A097PIJ6 |
Cytogenetics | 22q12.1 |
Synonyms | CTRCT23; CYRBA4; MCOPCT4 |
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, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008] |
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