Analytical Data
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Gene name
DERP6
- Application
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Alternative Names
DERP6；C17orf81；DERP6；Elongator complex Protein 5
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Species
E.coli
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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
P49277
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Expression Region
1-20aa
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AA Sequence
AIGSQPAAEAEAPFQISLMK
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Molecular Weight
28.2 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
DERP6 (Dermatopontin Enhancer Regulatory Protein 6) is a protein that has garnered attention in the field of molecular biology and genetic research due to its potential role in various biological processes. Initially identified in skin and connective tissues, DERP6 is believed to be involved in the regulation of extracellular matrix components, which are crucial for tissue structure and integrity. Research has suggested that DERP6 may play a pivotal role in skin homeostasis and wound healing, as well as in the modulation of inflammatory responses. Studies have indicated that alterations in DERP6 expression can be linked to several pathological conditions, including skin disorders and fibrosis. The recombinant form of DERP6 is of particular interest, as it allows for detailed investigations into the protein's functional properties and mechanisms of action. By producing DERP6 in a controlled laboratory setting, researchers aim to elucidate its interactions with other key molecules within the extracellular matrix and its potential therapeutic applications. This research contributes to a better understanding of skin biology and offers insights into novel strategies for treating diseases associated with abnormal skin and connective tissue functions. Overall, the study of DERP6 and its recombinant protein form holds promise for advancing both basic biological knowledge and potential clinical applications in dermatology and regenerative medicine.
