Beta-crystallin A4 (1-196, His-tag) Human Protein

Specifications

Product Data
Species	Human
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) 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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