Analytical Data
-
Gene name
CRYBB3
- Application
-
Alternative Names
CRYBB3; CRYB3Beta-crystallin B3; Beta-B3 crystallin) [Cleaved into: Beta-crystallin B3; N-terminally processed
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P26998
-
Expression Region
1-211aa
-
AA Sequence
MAEQHGAPEQ AAAGKSHGDL GGSYKVILYE LENFQGKRCE LSAECPSLTD SLLEKVGSIQ VESGPWLAFE SRAFRGEQFV LEKGDYPRWD AWSNSRDSDS LLSLRPLNID SPHHKLHLFE NPAFSGRKME IVDDDVPSLW AHGFQDRVAS VRAINGTWVG YEFPGYRGRQ YVFERGEYRH WNEWDASQPQ LQSVRRIRDQ KWHKRGRFPS S
-
Molecular Weight
24.2 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
CRYBB3, a gene encoding the βB3-crystallin protein, plays a significant role in maintaining lens transparency and providing structural stability in the eye. Alterations or mutations in CRYBB3 have been implicated in various forms of congenital cataracts and other eye disorders, making it a focal point in ocular research. The study of CRYBB3 recombinant protein is essential for understanding the functional implications of these mutations as well as the mechanisms underlying lens opacity. Advancements in recombinant protein technology enable the production of CRYBB3 in heterologous systems, allowing researchers to investigate its biochemical properties, structural characteristics, and interactions with other lens proteins. By characterizing the functional aspects of CRYBB3, we can gain insights into the pathogenesis of cataracts and develop potential therapeutic strategies. Moreover, studying CRYBB3 can contribute to the broader understanding of crystallin proteins and their evolutionary adaptations in different species. Research into CRYBB3 recombinant protein has the potential to bridge gaps in our knowledge about ocular health, paving the way for innovative approaches in diagnosing and treating lens-related diseases.
