Analytical Data
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Gene name
CRYZ
- Application
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Alternative Names
CRYZ;Quinone oxidoreductase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08257
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Expression Region
2-329aa
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AA Sequence
ATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG SQYPLEKVAE AHENIIHGSG ATGKMILLL
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CRYZ, or crystallin zeta, is a member of the crystallin family of proteins, primarily found in vertebrate lenses. It plays a crucial role in maintaining lens transparency and refractive properties, which are essential for proper vision. Research into CRYZ has gained momentum due to its potential implications in understanding eye diseases, particularly cataracts, which can arise from alterations in crystallin structure or function. The study of CRYZ as a recombinant protein has opened new avenues for investigating its biochemical properties, folding mechanisms, and interaction with other lens proteins. Furthermore, recombinant CRYZ can be utilized to explore the molecular basis of its chaperone-like activity, which may help prevent protein aggregation—a common issue associated with lens opacification. By characterizing the structure and functional dynamics of CRYZ, researchers aim to elucidate the protective mechanisms it employs within the ocular environment. This knowledge could pave the way for innovative therapeutic strategies to combat lens-related disorders. Overall, CRYZ’s significance in both normal lens function and its role in cataractogenesis positions it as a pivotal focus in ongoing studies aimed at understanding and eventually mitigating the impact of age-related and hereditary eye conditions.
