Analytical Data
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Gene name
DERP1
- Application
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Alternative Names
DERP1；Peptidase 1
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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
P08176
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Expression Region
99-320aa
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AA Sequence
TNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVIL
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Molecular Weight
41.0 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
DERP1, or Dermatopontin 1, is a protein that has garnered attention in recent years for its potential roles in various biological processes, including cell adhesion, migration, and tissue remodeling. It is particularly relevant in the context of skin development and repair, as it is involved in the organization of the extracellular matrix (ECM). Research has shown that alterations in DERP1 expression can lead to pathological conditions, such as fibrosis and skin disorders. Its reorganization during wound healing processes suggests that it could serve as a biomarker for skin health and a therapeutic target for regenerative medicine. Furthermore, studies have highlighted its involvement in inflammatory responses and immune regulation, suggesting that DERP1 may have broader implications in disease pathogenesis beyond dermatological applications. The reconstruction of DERP1 in laboratory settings allows researchers to explore its functional mechanisms at a molecular level, aiding in the identification of therapeutic strategies for conditions linked to abnormal DERP1 activity. Understanding the structure-function relationship of DERP1 through recombinant protein technologies could provide insights into its role in both normal physiology and disease states, emphasizing the need for comprehensive studies to elucidate its contributions across various biological systems. This research not only expands our knowledge of DERP1 but also opens avenues for potential clinical applications, highlighting its significance in both dermatological and systemic diseases.
