Analytical Data
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Gene name
UBC5A
- Application
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Alternative Names
E2 ubiquitin-conjugating enzyme 5A; Ubiquitin carrier protein 5a; OsUBC5a; Ubiquitin-protein ligase 5A
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Species
Oryza sativa subsp. japonica
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8S920
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Expression Region
1-147aa
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Molecular Weight
23.6 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
UBC5A, a member of the ubiquitin-conjugating enzyme family, plays a crucial role in the ubiquitin-proteasome pathway, which is essential for regulating protein degradation, signaling, and various cellular processes. The study of UBC5A is significant because it is involved in the modification of substrate proteins through ubiquitination, thereby influencing cell cycle progression, DNA repair, and stress responses. Aberrations in UBC5A function have been implicated in various diseases, including cancer, neurodegenerative disorders, and immune dysfunction. Recent advancements in understanding the structure and dynamics of UBC5A have shed light on its substrate specificity and regulatory mechanisms. Moreover, exploring its interactions with E3 ligases and other cellular factors provides insights into the intricate networks governing cellular homeostasis. Therefore, the characterization and functional analysis of recombinant UBC5A protein is an area of intense research, aimed at uncovering its potential as a therapeutic target and enhancing our understanding of ubiquitin-related cellular pathways. By employing techniques such as X-ray crystallography, mass spectrometry, and biochemical assays, researchers aim to elucidate the mechanistic details of UBC5A-mediated ubiquitination and its broader implications in health and disease.
