Recombinant Apis mellifera Melittin (MELT)

Code CSB-YP355665DNK
MSDS
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Source Yeast
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Code CSB-EP355665DNK-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP355665DNK
MSDS
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Source Baculovirus
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Code CSB-MP355665DNK
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
MELT
Uniprot No.
Alternative Names
MELT; Melittin; MEL; MLT; Allergen Api m 3; Allergen Api m III; allergen Api m 4
Species
Apis mellifera (Honeybee)
Expression Region
44-69
Target Protein Sequence
GIGAVLK VLTTGLPALI SWIKRKRQQ
Protein Length
Cytoplasmic domain
Tag Info
Tag type will be determined during the manufacturing process.
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.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
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
  1. this study shows that melittin constrains the expression of identified key genes associated with bladder cancer PMID: 29854840
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. 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

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Subcellular Location
Secreted. Target cell membrane.
Protein Families
Melittin family
Tissue Specificity
Expressed by the venom gland.
Database Links

KEGG: ame:406130

STRING: 7460.GB10355-PA

UniGene: Ame.1212

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