Analytical Data
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Gene name
CRYGD
- Application
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Alternative Names
CRYGD；CRYG4;Gamma-crystallin D
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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
P07320
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Expression Region
1-174aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGKITLYEDRGFQGRHYECSSDHPNLQPYL SRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCR LIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGS WVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS
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Molecular Weight
23 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
CRYGD, or crystallin gamma D, is a member of the gamma-crystallin family, primarily expressed in the lens of the eye, where it plays a critical role in maintaining transparency and refractive properties essential for proper vision. The study of CRYGD recombinant proteins has garnered significant attention due to their involvement in various eye disorders, including hereditary cataracts, which can lead to vision impairment or blindness. Research into CRYGD focuses on understanding its structure-function relationship, post-translational modifications, and aggregation mechanisms that may result in lens opacification. Moreover, insights gained from the characterization of CRYGD recombinant proteins can contribute to the development of therapeutic strategies for cataract treatment and prevention, as well as potential applications in tissue engineering and regenerative medicine. This research underscores the importance of gamma-crystallins not only as structural proteins but also as critical players in cellular processes related to lens health and integrity. Understanding the molecular dynamics of CRYGD offers a promising avenue for advancing our knowledge of ocular biology and addressing vision-related pathologies.
