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Cecropin B

≥97% (HPLC), powder

Empirical Formula (Hill Notation):
Número CAS:
Peso molecular:
Número MDL:

Nível de qualidade



≥97% (HPLC)



Modo de ação

cell membrane | interferes

espectro de atividade do antibiótico


temperatura de armazenamento




InChI key


Amino Acid Sequence


Descrição geral

Cecropin B is an antimicrobial peptide present in the hemolymph of the silk moth, Hyalophora cecropia. It is a member of the Cecropin class and possesses an α-helix-like structure. 
Chemical structure: peptide


Cecropin B has been used as an antibiotic peptide to study its cytotoxic potential in breast adenocarcinoma and mesothelioma cell lines. It has also been used as an antimicrobial peptide to test the susceptibility of the Photorhabdus variants in minimal inhibitory concentration (MIC) assays.

Ações bioquímicas/fisiológicas

Cecropin B is known for its antimicrobial activity. It displays antitumor effects in hepatocellular carcinoma, lymphoma, and leukemia cell lines.
Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine.

Outras notas

Lyophilized from 0.1% TFA in H2O

Código de classe de armazenamento

13 - Non Combustible Solids



Ponto de fulgor (ºF)

Not applicable

Ponto de fulgor (ºC)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificado de análise

Certificado de origem

Frank Rasche et al.
FEMS microbiology ecology, 56(2), 219-235 (2006-04-25)
A greenhouse experiment was performed to analyze a potential effect of genetically modified potatoes expressing antibacterial compounds (attacin/cecropin, T4 lysozyme) and their nearly isogenic, nontransformed parental wild types on rhizosphere bacterial communities. To compare plant transformation-related variations with commonly accepted
Z Abi Khattar et al.
Journal of bacteriology, 191(22), 7063-7073 (2009-09-22)
The dlt operon encodes proteins that alanylate teichoic acids, the major components of cell walls of gram-positive bacteria. This generates a net positive charge on bacterial cell walls, repulsing positively charged molecules and conferring resistance to animal and human cationic
Nayanoori Harikrishna et al.
Journal of vector borne diseases, 49(1), 19-22 (2012-05-16)
In the past 60 years, antibiotics have been critical in the fight against infectious diseases caused by bacteria and other microbes. Development of resistance to the antibiotics is emerging as a major public health issue which has resulted in the
Fuxian Yu et al.
Biotechnology letters, 32(5), 669-673 (2010-01-05)
Antibacterial peptides have a broad range of antibacterial properties that makes them highly toxic for expression in Escherichia coli. For prepare an antiserum to detect these peptides, we developed a cecropin B mutant with a green fluorescent protein fusion partner
Hai-tao Ren et al.
Zhonghua shao shang za zhi = Zhonghua shaoshang zazhi = Chinese journal of burns, 22(6), 445-447 (2007-04-19)
To investigate the antibacterial effect of a particular antimicrobial peptide Cecropin B(CB) on Pseudomonas aeruginosa infection of wound in mice. Thirty ICR mice were enrolled in the study, and the Pseudomonas aeruginosa infection model was reproduced by excision of the

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