Analytical Data
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Gene name
NET
- Application
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Alternative Names
NET；NET；SAP2；ETS domain-containing Protein Elk-3
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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
P41970
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Expression Region
1-407aa
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AA Sequence
MESAITLWQFLLQLLLDQKHEHLICWTSNDGEFKLLKAEEVAKLWGLRKNKTNMNYDKLSRALRYYYDKNIIKKVIGQKFVYKFVSFPEILKMDPHAVEISRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSTSEAAAASAFLASSVSAKISSLMLPNAASISSASPFSSRSPSLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGLLLTPSPLLSSIHFWSSLSPVAPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS
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Molecular Weight
44.2 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
The study of NET restructured proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology, medicine, and materials science. NETs, or Neutrophil Extracellular Traps, are extracellular structures composed of DNA and proteins that are released by neutrophils in response to pathogens. Recent research has shown that these structures play critical roles not only in the immune response but also in various pathological conditions. The manipulation and reorganization of NET proteins offer innovative strategies for drug delivery systems, targeted therapeutics, and advanced biomaterials. Furthermore, understanding the underlying mechanisms of NET formation and degradation can provide insights into chronic inflammatory diseases, autoimmune disorders, and cancer progression. As researchers delve deeper into the interplay of NETs with other cellular components and their role in disease mechanisms, the potential for developing novel therapeutic strategies that leverage NET protein restructuring continues to expand, highlighting the need for ongoing investigation in this promising area of study.
