Analytical Data
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Gene name
UFM1
- Application
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Alternative Names
UFM1；C13orf20；Ubiquitin-fold modifier 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
P61960
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Expression Region
1-83aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVG
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Molecular Weight
11 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
UFM1 (Ubiquitin-fold Modifier 1) is a highly conserved protein in eukaryotic cells, playing a crucial role in various cellular processes, including protein modification, stress response, and cell survival. UFM1 shares structural similarities with ubiquitin but functions through a distinct conjugation system, which involves the attachment of UFM1 to target proteins via a process called ufmylation. This modification is vital for regulating protein stability and promoting cellular adaptation to stressors, such as hypoxia or oxidative stress. Recent studies have highlighted UFM1's involvement in critical biological pathways, including autophagy, cell cycle regulation, and immune responses. Dysregulation of UFM1 has been implicated in several diseases, including cancer and neurodegenerative disorders, making it a potential therapeutic target. As researchers delve deeper into the mechanisms of ufmylation and its impact on cellular functions, understanding UFM1's role could unveil novel insights into disease mechanisms and lead to the development of innovative treatments. Overall, UFM1 research not only enhances our understanding of post-translational modifications but also opens new avenues for therapeutic exploration in various health conditions.
