Analytical Data
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Gene name
SPRR4
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96PI1
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Expression Region
Met1~Lys79
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Molecular Weight
13kDa
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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
SPRR4 (Small Proline-Rich Protein 4) is a member of the small proline-rich protein family, which plays a significant role in various biological processes, including epithelial differentiation, wound healing, and responses to stress. Its expression is primarily observed in stratified squamous epithelia, where it contributes to barrier function and cellular integrity. Research into SPRR4 has garnered attention due to its potential implications in skin disorders, such as psoriasis and keratoderma, where its dysregulation may lead to impaired epithelial homeostasis. Moreover, SPRR4 has been implicated in the process of tumorigenesis; its altered expression could influence cancer cell behavior and the microenvironment. The recombinant expression of SPRR4 protein allows for in-depth studies of its functional properties, interactions with other proteins, and mechanisms of action at the cellular level. By producing SPRR4 in a controlled laboratory setting, researchers aim to elucidate its role in epidermal biology and explore its potential as a therapeutic target or biomarker for skin-related diseases and conditions. Understanding SPRR4's structure-function relationship is crucial for developing novel strategies to modulate its activity in clinical applications, representing a promising area of investigation in the field of molecular biology and dermatology.
