Summary:
Recombinant human CRYBA4 protein
Cat：P05693
| 【Derived From】： E.coli |
| 【Endotoxin】： Not measured |
| 【Amino Acid】： 1-197aa |
| 【Purity】： ≥85% by SDS-PAGE. |
| 【Name】： CRYBA4 |
| 【Full Name】： crystallin，beta A4 |
| 【Uniprot】： P53673 |
| 【Gene ID】： 1413 |
| 【Species Reactivity】： Human Mouse Rat (Bovine Dog Chicken) |
| 【Mol Mass】： 22.4kDa |
| 【Application】： Immunology research |
| 【Purification】： NI-NTA affinity purification |
| 【Bioactive】： N0 |
| 【Tag】： With a 6×His tag at the N/C-terminus. |
| 【Concentration】： 1mg/ml by SDS-PAGE. |
Store:
| 【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.) |
| 【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks， stored at < -20℃ for 1 year. |
| 【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0. |
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-crys
Verified picture
