Analytical Data
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Gene name
FLG2
- Application
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Alternative Names
FLG2；IFPS；Filaggrin-2
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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
Q5D862
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Expression Region
全长
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AA Sequence
full
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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
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Protein Description
FLG2 (Filaggrin 2) is a crucial protein involved in the keratinocyte differentiation process and plays a significant role in maintaining skin barrier function. It is a member of the filaggrin family, which contributes to the aggregation of keratin filaments, thereby providing structural integrity to the epidermis. With increasing evidence linking FLG2 dysfunction to various skin disorders such as atopic dermatitis, psoriasis, and ichthyosis, researchers have begun to explore its molecular mechanisms and therapeutic potential. The study of FLG2 recombinant proteins has gained traction as a means to better understand its biophysical properties and interactions within cellular environments. By producing FLG2 in a recombinant form, scientists can investigate its structural characteristics, functional roles, and possible implications for skin health. Additionally, such studies aim to elucidate the post-translational modifications that govern FLG2's stability and activity, as well as to explore its potential as a biomarker for disease states. The ongoing research into FLG2 recombinant proteins not only enhances our understanding of skin biology but also paves the way for novel therapeutic strategies targeting skin barrier dysfunctions, which are prevalent in many dermatological conditions. Thus, the investigation of FLG2 holds promise for advancing skin health and developing innovative treatments.
