Analytical Data
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Gene name
SPRR2G
- Application
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Alternative Names
SPRR2G; Small proline-rich protein 2G; SPR-2G
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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
Q9BYE4
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Expression Region
1-73aa
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AA Sequence
MSYQQQQCKQ PCQPPPVCPT PKCPEPCPPP KCPEPYLPPP CPPEHCPPPP CQDKCPPVQP YPPCQQKYPP KSK
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Molecular Weight
8.1 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
The SPRR2G (Small Proline-Rich Protein 2G) is a member of the small proline-rich protein family, which plays a crucial role in various biological processes, including epithelial cell differentiation, tissue repair, and response to stress. Research into SPRR2G has gained importance due to its potential implications in skin biology and various pathophysiological conditions, such as skin disorders and cancer. SPRR2G is primarily expressed in the epidermis, where it contributes to the structural integrity of the skin by associating with keratin intermediate filaments and other cytoskeletal elements. Additionally, studies have shown that the expression of SPRR2G can be regulated by various stimuli, indicating its role in adaptive responses to environmental changes. Given its potential as a biomarker for certain skin diseases and its involvement in the wound healing process, the recombinant production of SPRR2G protein has become a focal point in biomedical research. Researchers aim to explore its structure-function relationships and therapeutic potential by utilizing recombinant DNA techniques to produce SPRR2G in various expression systems. This approach facilitates the investigation of its biochemical properties, cellular interactions, and potential pathways through which it exerts its effects. Understanding SPRR2G at a molecular level could yield insights into its role in skin health and disease, thereby opening avenues for the development of targeted therapies for related conditions. Overall, the study of recombinant SPRR2G promotes a deeper comprehension of skin biology and its associated challenges, ultimately contributing to advancements in dermatological research and treatment strategies.
