Analytical Data
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Gene name
gelE
- Application
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Alternative Names
gelE；CAD；DFF2；DFF40；DNA fragmentation factor subunit beta
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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
Q833V7
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Expression Region
193-510aa
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AA Sequence
VGSEVTLKNSFQVAFNVPVEKSNTGIALHGTDNTGVYHAVVDGKNNYSIIQAPSLVALNQNAVDAYTHGKFVKTYYEDHFQRHSIDDRGMPILSVVDEQHPDAYDNAFWDGKAMRYGETSTPTGKTYASSLDVVGHEMTHGVTEHTAGLEYLGQSGALNESYSDLMGYIISGASNPEIGADTQSVDRKTGIRNLQTPSKHGQPETMAQYDDRARYKGTPYYDQGGVHYNSGIINRIGYTIIQNLGIEKAQTIFYSSLVNYLTPKAQFSDARDAMLAAAKVQYGDEAASVVSAAFNSAGIGAKEDIQVNQPSESVLVNE
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Molecular Weight
47.5 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
GelE recombinant proteins have garnered significant attention in recent years due to their versatile applications in biotechnology and medicine. GelE, a gelatinase encoded by certain bacteria, is known for its ability to degrade gelatin and collagen, which are essential components of the extracellular matrix in various tissues. This enzymatic activity makes GelE a valuable tool for tissue engineering and regenerative medicine, where scaffold materials need to be broken down or modified. Research into GelE recombinant proteins focuses on optimizing their expression systems for enhanced yield and activity, studying their structural properties, and exploring their potential therapeutic applications. Additionally, due to their role in microbial pathogenesis, GelE-based studies contribute to understanding infection mechanisms, paving the way for the development of novel antibacterial strategies. As a result, GelE recombinant proteins are not only important for fundamental research but also for practical applications in developing diagnostic tools and therapeutic agents, making them a focal point in the intersection of molecular biology and clinical medicine.
