Analytical Data
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Gene name
eno
- Application
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Alternative Names
eno；Enolase 4
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Species
Human
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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
Q2YSE8
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Expression Region
1-434aa
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AA Sequence
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSKRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK
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Molecular Weight
54.0 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
Enolase (ENO) is a glycolytic enzyme involved in the conversion of 2-phosphoglycerate to phosphoenolpyruvate, playing a crucial role in cellular metabolism. It exists in multiple isoforms, with ENO1 being the most widely studied due to its involvement in various biological processes beyond metabolism, including cell proliferation, apoptosis, and stress response. Recent research has highlighted ENO1's potential role as an oncofetal protein, which is expressed in higher levels during tumorigenesis, making it a candidate for cancer diagnostics and therapeutics. Moreover, ENO1 has been implicated in the regulation of key signaling pathways, influencing tumor cell behavior and interaction with the tumor microenvironment. Understanding the structure-function relationship of ENO1, and its regulatory mechanisms, is essential for developing targeted therapies in cancer treatment. Additionally, ENO1’s interactions with other cellular proteins have garnered interest in elucidating its role in various diseases. The study of ENO's recombinant protein has advanced through techniques such as X-ray crystallography and cryo-electron microscopy, providing insights into its enzymatic function and potential ligand-binding sites. Overall, ENO research represents a significant intersection of enzymology, cancer biology, and therapeutic development, warranting further exploration to harness its potential in clinical applications.
