Analytical Data
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Gene name
CATHL1
- Application
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Alternative Names
CATHL1；BAC1；Cathelicidin-1
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Species
Bovine
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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
P22226
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Expression Region
144-155aa
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AA Sequence
RLCRIVVIRVCR
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Molecular Weight
30.4 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
CATHL1 (Cationic Antimicrobial Peptide with a CATHL1 Domain) is a member of the cathelicidin family, known for its role in innate immunity, particularly in host defense against microbial infections. Its antimicrobial properties and ability to modulate immune responses have drawn significant interest in biomedical research. The study of CATHL1 recombinant protein is driven by its potential applications in therapeutic strategies, particularly in treating infections caused by antibiotic-resistant bacteria. Research has shown that CATHL1 exhibits broad-spectrum antimicrobial activity, not only against bacteria but also fungi and viruses, making it a candidate for developing novel antimicrobial agents. Furthermore, CATHL1 has been linked to wound healing and tissue regeneration, highlighting its multifunctional roles in the body. Understanding the structure-function relationship of CATHL1 through recombinant protein studies allows researchers to optimize its properties for therapeutic use, assess its effectiveness in various biological contexts, and explore its mechanisms of action in immune modulation. As antibiotic resistance continues to pose a significant global health threat, the exploration of CATHL1 and its recombinant forms may pave the way for innovative solutions in antimicrobial therapy and enhance the understanding of host-pathogen interactions.
