Analytical Data
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Gene name
UFSP1
- Application
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Alternative Names
UFSP1；Inactive Ufm1-specific protease 1
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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
Q6NVU6
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Expression Region
1-142aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGDKPPG FRGSRDWIGC VEASLCLAHF GGPQGRLCHV PRGVGLHGEL ERLYSHFAGG GGPVMVGGDA DARSKALLGV CVGSGTEAYV LVLDPHYWGT PKSPSELQAA GWVGWQEVSA AFDPNSFYNL CLTSLSSQQQ QRTLD
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Molecular Weight
17 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
UFSP1 (Ubiquitin-fold Modifier 1) is a protein that plays a critical role in the post-translational modification of proteins through the ubiquitin-proteasome pathway. This pathway is essential for regulating various cellular processes, including protein degradation, cell cycle progression, and signal transduction. Recent studies have highlighted UFSP1's involvement in modulating protein stability and function, particularly in the context of stress responses and disease mechanisms, such as cancer and neurodegenerative disorders. The interest in UFSP1 has grown due to its potential as a therapeutic target, given its regulatory effect on protein levels that contribute to pathophysiological conditions. Researchers have begun investigating the structure-function relationship of UFSP1, aiming to elucidate its mechanism of action and interaction with other cellular components. The development of recombinant UFSP1 protein allows for in-depth studies of its biochemical properties and biological activities, paving the way for potential applications in drug development and understanding disease biology. As such, UFSP1 represents an important focus of research in cellular and molecular biology, with implications for therapeutic interventions in diseases linked to dysregulated protein homeostasis.
