Analytical Data
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Gene name
LEAP2
- Application
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Alternative Names
LEAP2；Liver-expressed antimicrobial peptide 2
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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
Q969E1
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Expression Region
38-77aa
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AA Sequence
MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE
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Molecular Weight
36.1 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
LEAP2 (Liver Expressed Antimicrobial Peptide 2) is a member of the family of antimicrobial peptides (AMPs), which are crucial components of the innate immune system. Discovered as a protein predominantly expressed in the liver, LEAP2 has gained attention due to its potential role in modulating immune responses and its involvement in various physiological processes. Research has indicated that LEAP2 exhibits antimicrobial activity against a range of pathogens, indicating its significance in protecting the host from infections. Additionally, studies suggest that LEAP2 may interact with various receptors and influence metabolic functions, linking it to conditions such as obesity and insulin resistance. The recombinant production of LEAP2 opens avenues for in-depth studies into its structure-function relationships and therapeutic applications. As researchers explore its mechanisms of action, LEAP2 is being investigated not only for its antimicrobial properties but also for its potential insights into metabolic diseases and inflammatory conditions. Investigating LEAP2 through recombinant protein technologies allows for higher yields and purer forms of the protein, facilitating advanced research into its biological roles and potential clinical applications. This growing body of work underscores the importance of LEAP2 as a multifunctional player in immune defense and metabolic regulation.
