Analytical Data
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Gene name
ugl
- Application
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Alternative Names
ugl；FN；Fibronectin
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Species
E.coli
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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
Q9RC92
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Expression Region
1-377aa
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AA Sequence
MWQQAIGDALGITARNLKKFGDRFPHVSDGSNKYVLNDNTDWTDGFWSGILWLCYEYTGDEQYREGAVRTVASFRERLDRFENLDHHDIGFLYSLSAKAQWIVEKDESARKLALDAADVLMRRWRADAGIIQAWGPKGDPENGGRIIIDCLLNLPLLLWAGEQTGDPEYRRVAEAHALKSRRFLVRGDDSSYHTFYFDPENGNAIRGGTHQGNTDGSTWTRGQAWGIYGFALNSRYLGNADLLETAKRMARHFLARVPEDGVVYWDFEVPQEPSSYRDSSASAITACGLLEIASQLDESDPERQRFIDAAKTTVTALRDGYAERDDGEAEGFIRRGSYHVRGGISPDDYTIWGDYYYLEALLRLERGVTGYWYERGR
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Molecular Weight
42.8 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
Related Products
Protein Description
Ugl (Ubiquitin-like protein) recombinant proteins have garnered significant attention in the fields of molecular biology and biotechnology due to their critical roles in cellular processes. These proteins are often involved in the regulation of protein degradation, cell cycle progression, and response to stress, functioning through mechanisms similar to ubiquitin. The study of Ugl recombinant proteins is essential for understanding their structure-function relationships and the pathways they influence, which can have profound implications for disease models, particularly in cancer and neurodegenerative disorders. Advances in techniques such as CRISPR-Cas9 gene editing and recombinant DNA technology have facilitated the expression and purification of Ugl proteins, allowing researchers to investigate their biological activities in detail. Additionally, the therapeutic potential of Ugl proteins is being explored, as manipulating their signaling pathways could lead to novel treatment strategies. Overall, the research on Ugl recombinant proteins not only expands our fundamental knowledge of cellular biology but also opens new avenues for therapeutic development in various diseases.
