Analytical Data
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Gene name
UBE1L2/UBA6
- Application
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Alternative Names
UBE1L2; MOP-4; Monocyte protein 4; Ubiquitin-Activating Enzyme E1-Like 2; Ubiquitin-activating enzyme E1-like protein 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0AVT1
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Expression Region
Met1~Ile181
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Molecular Weight
24kDa
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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
UBE1L2 (also known as UBA6) is a member of the E1 ubiquitin-activating enzyme family, which plays a crucial role in the ubiquitin-proteasome system, a key regulatory pathway for protein degradation and cellular homeostasis. This enzyme is involved in the conjugation of ubiquitin to target proteins, marking them for degradation or signaling pathways. Recent studies have highlighted UBE1L2's unique functions compared to other E1 enzymes, including its distinct substrate specificity and regulatory mechanisms. Given the importance of ubiquitination in various biological processes, including cell cycle regulation, DNA repair, and response to stress, UBE1L2 has emerged as a potential player in diseases such as cancer and neurodegenerative disorders. Furthermore, its atypical behavior in mediating non-canonical ubiquitination suggests new avenues for therapeutic intervention. The recombinant expression of UBE1L2/UBA6 is critical for characterizing its enzymatic activity, understanding its substrate interactions, and exploring its biological functions. This research is vital for deciphering the complexities of ubiquitination and may provide insights into novel strategies for treating diseases associated with dysregulated protein homeostasis.
