Analytical Data
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Gene name
FLJ11011
- Application
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Alternative Names
FLJ11011; hUBC 16; hUBC16; Probable ubiquitin conjugating enzyme E2 W; Probable ubiquitin-conjugating enzyme E2 W; UBC 16; UBC-16; UBC16; UBE 2W; ube2w; UBE2W_HUMAN; Ubiquitin carrier protein W; Ubiquitin conjugating enzyme 16
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96B02
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Expression Region
1-151aa
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AA Sequence
MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC
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Molecular Weight
33.3 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
The FLJ11011 protein, also known as the hypothetical protein, is of significant interest in molecular biology due to its potential role in various cellular processes. Despite being classified as "hypothetical," initial studies have suggested its involvement in fundamental biological functions, making it a candidate for further investigation. Found in a variety of organisms, FLJ11011’s expression patterns and sequence homology indicate it may participate in diverse regulatory pathways. Notably, the lack of extensive prior research on this protein highlights the need for exploring its structure-function relationship. Advances in recombinant DNA technology have facilitated the production of FLJ11011 as a recombinant protein, allowing for detailed biochemical analysis and characterization. Understanding the protein's structure may reveal insights into its function and interaction with other biomolecules. Furthermore, FLJ11011 could possess implications in health and disease, including roles in signal transduction, metabolic regulation, or even as a biomarker for certain conditions. By employing techniques such as X-ray crystallography and mass spectrometry, researchers aim to elucidate the functional characteristics of FLJ11011, paving the way for future studies that could unveil therapeutic applications. Therefore, investigating FLJ11011 is not only crucial for expanding our understanding of unexplored proteins but also for its potential implications in biotechnology and medicine.











