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M2272 Sigma

Melittin from honey bee venom

≥85% (HPLC)

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Description

Amino Acid Sequence

Gly-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile-Ser-Trp-Ile-Lys-Arg-Lys-Arg-Gln-Gln-NH2

Biochem/physiol Actions

Binds calmodulin in a Ca2+-dependent manner; inhibits Na+-K+-ATPase.

Melittin acts as an anti-coagulating protein by increasing the time of blood clotting in vitro. Melittin inhibits the activity of S100 calcium-binding protein B (S100B) and plays a vital role in Epilepsy treatment.

Other Notes

The principle hemolytic component of honeybee venom.

Packaging

1, 5, 25 mg in glass bottle

Application

Melittin from honey bee venom has been used:
• In 3-(4, 5-dimethyl thiazol-2-yl)-2,5diphenyl tetrazolium bromide (MTT) assay to determine its cytotoxicity effect on the growth of human cell lines.
• To study the anti-microbial activity of melittin on the growth of Borrelia burgdorferi in in vitro conditions.
• As a positive control in hemolysis assay and as a cytotoxic agent against HeLa cells.

General description

Melittin is hydrophobic in nature except for a region with Lys-Arg-Lys-Arg sequence near C-terminal end. This structural characteristic makes melittin a highly surface-active and a powerful, direct haemolytic agent.† The encoded protein containins 26 amino acids. Monomeric form of melittin has a molecular weight of 2,840 Daltons and tetrameric form has molecular weight of approximately 12,500 Daltons.

Price and Availability


All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

RIDADR 
UN 3462 6.1 / PGI
WGK Germany 
3
RTECS 
OS3960000
Protocols & Articles

Articles

Antimicrobial Peptides

With bacterial resistance and emerging infectious diseases becoming potential threats to humans, ribosomally synthesized antimicrobial peptides have become a promising focus area in antibiotic resear...
Chloe McClanahan
BioFiles 2009, 4.3, 4.
Keywords: Antibiotics, Antimicrobials, Antiparasitics, Antivirals, Apoptosis, Cancer, Clinical, Diseases, Environmental, Fermentation, Food Safety, Gene expression, Genetic, Genetics, Infectious Diseases, Microbiology, Peptide synthesis, Pesticides, Respiratory

Peer-Reviewed Papers
15

References

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