Analytical Data
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基因名
Cathelicidin-4
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简介
Cathelicidin-4/CATHL4 protein has potent bactericidal activity and can effectively target Staphylococcus aureus and Escherichia coli. This antibacterial ability makes cathelicidin-4 an important innate immune effector that contributes to host defense against bacterial pathogens. Cathelicidin-4/CATHL4 Protein, Bovine (His-SUMO) is the recombinant bovine-derived Cathelicidin-4/CATHL4 protein, expressed by E. coli , with N-His, N-SUMO labeled tag.
- Application
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别名
CATHL4; Cathelicidin-4; Indolicidin
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种属
Bovine
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表达系统
E. coli
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标签
N-His;N-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P33046
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表达区间
I131-R143
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蛋白长度
Full Length of Mature Peptide
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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Protein Description
Cathelicidin-4 (CATH-4) is a member of the cathelicidin family of antimicrobial peptides, which play a crucial role in the innate immune response of various organisms. Initially discovered in specific vertebrates, such as humans and mice, CATH-4 is known for its potent antimicrobial properties against a wide range of pathogens, including bacteria, viruses, and fungi. Its mechanism of action involves disrupting microbial membranes, leading to cell lysis. Research into CATH-4 is particularly relevant due to the increasing prevalence of antibiotic-resistant infections, making the development of new antimicrobial agents imperative. Furthermore, CATH-4 exhibits additional functions, including immunomodulatory effects, promoting wound healing and modulating inflammatory responses. Studies have shown that this peptide can enhance the activity of other immune cells, thus contributing to a more comprehensive approach to infection control. Additionally, recombinant technology has enabled the production of CATH-4 in vitro, facilitating detailed studies on its structure-function relationship and therapeutic potential. Investigating CATH-4 not only contributes to the fundamental understanding of innate immunity but also opens avenues for the development of novel therapeutics in combating resistant microbial strains and improving clinical outcomes in infectious diseases. As such, CATH-4 represents a promising candidate in the search for effective antimicrobial therapies and serves as a critical focus for further research in immunology and infectious disease management.
