Recombinant Apis Mellifera Melittin (MELT)

Name: Recombinant Apis Mellifera Melittin (MELT)
Brand: Beta LifeScience
SKU: BLC-11023P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Recombinant proteins fall special offers - tag-free proteins

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Product Overview

Description	Recombinant Apis Mellifera Melittin (MELT) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P01501
Target Symbol	MELT
Synonyms	MELT; Melittin; MEL; MLT; Allergen Api m 3; Allergen Api m III; allergen Api m 4
Species	Apis mellifera (Honeybee)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	GIGAVLKVLTTGLPALISWIKRKRQQ
Expression Range	44-69aa
Protein Length	Full Length of Mature Protein
Mol. Weight	2.8 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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.
Subcellular Location	Secreted. Target cell membrane.
Protein Families	Melittin family
Database References	KEGG: ame:406130 STRING: 7460.GB10355-PA UniGene: 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.