MELT Antibody

Code CSB-PA355665ZA01DNK
Size US$299
Image
  • Western Blot
    Positive WB detected in: recombinant protein
    All lanes: MELT Antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 17 kDa
    Observed band size: 17 kDa
The Latest Promotion Free Antibody trial simple
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Full Product Name
Rabbit anti-Apis mellifera (Honeybee) MELT Polyclonal antibody
Uniprot No.
Target Names
MELT
Alternative Names
Melittin (Allergen Api m 3) (Allergen Api m III) (allergen Api m 4), MELT
Raised in
Rabbit
Species Reactivity
Apis mellifera
Immunogen
Recombinant Apis mellifera MELT protein (44-69aa)
Immunogen Species
Apis mellifera (Honeybee)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

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

Show More

Hide All

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

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1