Analytical Data
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Gene name
SPRR1A
- Application
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Alternative Names
SPRR1A；Cornifin-A
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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
P35321
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Expression Region
1-89aa
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AA Sequence
MNSQQQKQPCTPPPQPQQQQVKQPCQPPPQEPCIPKTKEPCHPKVPEPCHPKVPEPCQPKVPEPCQPKVPEPCPSTVTPAPAQQKTKQK
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Molecular Weight
17.3 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
SPRR1A (small proline-rich protein 1A) is a member of the small proline-rich protein family, which plays a crucial role in keratinocyte differentiation and is predominantly expressed in the epidermis. Research into SPRR1A has gained attention due to its potential implications in skin physiology and pathology, particularly in wound healing and skin-related disorders. Studies have shown that SPRR1A is involved in the maintenance of skin barrier function and responds to various environmental stressors, suggesting its protective roles in skin defense mechanisms. The understanding of SPRR1A’s structure and function could provide insights into its regulatory pathways and interactions with other proteins, which may lead to novel therapeutic strategies for conditions such as psoriasis, atopic dermatitis, and skin cancer. Given the increasing prevalence of such skin diseases, continued investigation into SPRR1A and its recombinant forms is essential for elucidating its biological functions and exploring its potential as a biomarker or a therapeutic target in dermatological research.
