Recombinant Apis mellifera Melittin (MELT)

Code: CSB-EP355665DNK

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Size:

20μg100μg1mg(1mg*1 or 500ug*2)

US$554

Quantity:

Express system: E.coli

Species: Apis mellifera (Honeybee)

Tag Info: Tag-Free

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Target Background

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

MELT

Uniprot NO.

P01501

Research Area

Cell Biology

Alternative Names

MELT; Melittin; MEL; MLT; Allergen Api m 3; Allergen Api m III; allergen Api m 4

Species

Apis mellifera (Honeybee)

Source

E.coli

Expression Region

44-69aa

Target Protein Sequence

GIGAVLKVLTTGLPALISWIKRKRQQ
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

2.8 kDa

Protein Length

Full Length of Mature Protein

Tag Info

Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Buffer

Tris-based buffer，50% glycerol

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Troubleshooting and FAQs

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Datasheet & COA

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Images

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Target Background

Function(From Uniprot)

Melittin: Main toxin of bee venom with strong hemolytic activity and antimicrobial activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self-association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore-forming activity.; Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.; Melittin-2: Has strong hemolytic activity.

Gene References into Functions

this study shows that melittin constrains the expression of identified key genes associated with bladder cancer PMID:29854840
Molecular dynamics simulation was performed to characterize the structure and interaction of melittin with lipid molecules in dimyristoylphosphatidylglycerol bilayers. The simulation results indicate that basic amino acid residues in melittin interact strongly with lipid head groups to generate a pseudo-transmembrane alignment. PMID:28165239
All-atom/coarse-grained approach simulations demonstrated a clear salt effect and a moderate temperature effect on aggregation and support the molten globule model of melittin aggregates. PMID:28636825
Taking uPA(1-43) amino acids specifically binding to uPAR as targeted part of fusion protein, and making use of antitumor activity of melittin, the recombinant fusion protein it was able to inhibit growth of ovarian tumors . PMID:25394558
These findings point to the preservation and, from more aqueous solvent conditions, the formation of an at least partially helical form of melittin in the gas-phase. PMID:21701716
isolation and biochemical characterization of melittin-S, an isoform of melittin comprising a Ser residue at the 10th position, from the venom of Africanized A. mellifera; seasonal variation in venom content of melittins PMID:20472009
This paper characterizes the quantitative parameters of the peptide-lipid interactions related to the mechanism of formation of toroidal pores by melittin, compared to the formation of barrel-stave pores by alamethicin. PMID:15035629
melittin is localized in a motionally restricted region in membranes; increasing unsaturation in membranes causes a considerable change in the secondary structure of membrane-bound melittin PMID:15471568
from a kinetics point of view, the formation of the alpha-helix is a consequence of the membrane insertion of melittin. The rate of melittin folding was found to be influenced by the lipid composition of the bilayer. PMID:15533303
Melittin does not block NF-kappa B-p50-DNA interactions; rather, the human cells tested show significantly increased mRNA levels of several inflammatory genes, elevated cyclooxygenase-2 protein levels, and release of large quantities of oxygen radicals. PMID:17579088
increases in plasma adrenaline, noradrenaline, vasopressin levels and renin activity mediate the pressor responses to melittin in normal and hypotensive conditions in rats PMID:17897713