Analytical Data
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Gene name
CRYGB
- Application
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Alternative Names
CRYGB；CRYG2；Gamma-crystallin B
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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
P07316
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Expression Region
1-175aa
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AA Sequence
MGKITFYEDRAFQGRSYECTTDCPNLQPYFSRCNSIRVESGCWMIYERPNYQGHQYFLRRGEYPDYQQWMGLSDSIRSCCLIPPHSGAYRMKIYDRDELRGQMSELTDDCISVQDRFHLTEIHSLNVLEGSWILYEMPNYRGRQYLLRPGEYRRFLDWGAPNAKVGSLRRVMDLY
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Molecular Weight
24.9 kDa
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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
CRYGB (Crystallin, Gamma B) is a member of the gamma-crystallin family, which plays a crucial role in maintaining lens transparency and refractive properties in the eye. These proteins are primarily expressed in the lens, where they contribute to the structural and functional integrity necessary for optimal vision. Research into CRYGB and its recombinant protein has garnered interest due to its potential implications in understanding cataract formation and other lens-related pathologies. Furthermore, CRYGB's stability and solubility characteristics make it a suitable candidate for studying protein folding and aggregation, which are critical factors in various ocular disorders. The recombinant expression of CRYGB allows for detailed biochemical analyses and the exploration of its interactions with other lens proteins, thus providing insights into the molecular mechanisms underlying lens clarity and the development of therapeutic approaches for lens opacities. Additionally, CRYGB serves as a model for studying protein disulfide bond formation and post-translational modifications, which are essential for the functional maturation of crystallins. Given the increasing incidence of cataracts globally, the study of CRYGB and its properties is not only important for basic science but also for developing novel strategies for preventing and treating lens-related diseases, highlighting its significance in both research and clinical contexts.
