Analytical Data
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Gene name
SPRR2F
- Application
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Alternative Names
SPRR2F; Small proline-rich protein 2F; SPR-2F
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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
Q96RM1
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Expression Region
1-72aa
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AA Sequence
MSYQQQQCKQ PCQPPPVCPA PKCPEPCPPP KCPEPCPPSK CPQSCPPQQC QQKCPPVTPS PPCQPKCPPK SK
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Molecular Weight
7.8 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
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Protein Description
SPRR2F (Small Proline-Rich Protein 2F) is a member of the small proline-rich protein family, which plays critical roles in cellular processes, particularly in epithelial tissues. Research on SPRR2F has gained attention due to its potential involvement in various physiological and pathological conditions, including skin development, wound healing, and cancer progression. This protein is expressed predominantly in the epidermis, where it contributes to the formation of the cornified envelope, a key structure in skin barrier function. The interest in SPRR2F has been further heightened by studies suggesting that its expression is altered in several skin disorders and malignancies, indicating a potential link between SPRR2F and cellular stress responses. Recombination techniques to produce SPRR2F as a recombinant protein provide a valuable tool for studying its structural and functional properties, facilitating insights into its biological roles. Understanding the molecular mechanisms underlying SPRR2F function can reveal its significance in skin biology and pathology, paving the way for potential therapeutic applications in skin-related diseases. Thus, the study of SPRR2F not only enhances our knowledge of small proline-rich proteins but also contributes to the broader understanding of epidermal biology and its implications for health and disease.
