Analytical Data
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Gene name
UBA5
- Application
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Alternative Names
UBA5；UBE1DC1；Ubiquitin-like modifier-activating enzyme 5
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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
Q9GZZ9
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Expression Region
1-404aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM
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Molecular Weight
47 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
UBA5, an E1-like enzyme, plays a crucial role in the ubiquitin-proteasome system, which regulates a variety of cellular processes including protein degradation, cell cycle, and stress responses. As a member of the UBA family, UBA5 is primarily involved in the activation of ubiquitin-like proteins. Recent studies have highlighted its significant role in the post-translational modification of proteins, particularly in relation to the amino-acid starvation response, DNA repair mechanisms, and the regulation of cellular homeostasis. Understanding the functional dynamics and structural properties of UBA5 can offer insights into its involvement in various diseases, such as cancer, neurodegenerative disorders, and other pathologies where protein misfolding and degradation are implicated. Research has demonstrated that UBA5 is essential for the conjugation of ubiquitin-like modifiers to target proteins, influencing their stability and function. As a result, UBA5 has emerged as a potential therapeutic target, with ongoing investigations aimed at elucidating its molecular mechanisms and interactions within the ubiquitin pathway. Overall, the study of UBA5 not only enhances our comprehension of fundamental cellular processes but also opens avenues for developing novel strategies in disease treatment by manipulating the ubiquitin-proteasome system.
