Need Assistance?
  • US & Canada:
    +
  • UK: +

Andropin

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Andropin is an antimicrobial peptide produced by Drosophila yakuba (Fruit fly). It has moderate antibacterial activity against Gram-positive bacteria.

Category
Functional Peptides
Catalog number
BAT-013183
CAS number
133425-01-1
Molecular Formula
C176H291N43O46S
Molecular Weight
3777.57
Synonyms
Anp; Ile-Phe-Val-Asp-Val-Leu-Asp-Asn-Val-Glu-Thr-Ala-Leu-His-Asn-Ala-Ala-Lys-Ala-Gly-Phe-Lys-Leu-Ile-Lys-Pro-Ile-Glu-Lys-Leu-Ile-Met-Pro-Lys
Appearance
Lyophilized Powder
Purity
≥97%
Sequence
IFVDVLDNVETALHNAAKAGFKLIKPIEKLIMPK
Storage
Store at -20°C
1. Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila
Atsuko Date-Ito, Kumiko Kasahara, Hiromi Sawai, Sadao I Chigusa J Mol Evol. 2002 May;54(5):665-70. doi: 10.1007/s00239-001-0062-5.
Andropin, which encodes an antibacterial protein, is closely linked to the Cecropin gene cluster of D. melanogaster. Andropin and Cecropins are considered to have originated from one common ancestor. However, the expression pattern of Andropin is distinct from that of Cecropins, being restricted to the adult male ejaculatory duct. To elucidate the evolutionary process of Andropin, we have sequenced Andropin genes from D. melanogaster and its closely related species. In D. melanogaster, the nucleotide diversity of Andropin is remarkably low compared to that of Cecropin. In contrast, nonsynonymous substitutions of Andropin are conspicuously frequent between species. From genomic Southern analysis, Andropin-like genes are present in at least the melanogaster species subgroup. The series of present results suggests that Andropin was born in the course of constructing the Drosophila Cecropin gene family and then started to evolve rapidly, in contrast to Cecropins.
2. Changes in plasma C1q, apelin and adropin concentrations in older adults after descending and ascending stair walking intervention
Trevor C Chen, et al. Sci Rep. 2021 Sep 3;11(1):17644. doi: 10.1038/s41598-021-96631-x.
This study compared changes in plasma complement component 1q (C1q), apelin and adropin concentrations in older obese women after descending (DSW) and ascending stair walking (ASW) training (n = 15/group) performed twice a week for 12 weeks, with gradual increases in exercise time from 5 to 60 min. Fasting blood samples were collected 3 days before the first and 4 days after the last training session. The improvements in the maximal voluntary isometric contraction (MVIC) strength of the knee extensors, functional physical fitness [e.g., 30-s chair stand (CS) performance], resting systolic blood pressure (SBP), insulin sensitivity [e.g., oral glucose tolerance test (OGTT)] and blood lipid profiles [e.g., total cholesterol (TC)] were greater (p < 0.05) in the DSW than ASW group. Plasma C1q decreased (- 51 ± 30%), and apelin (23 ± 15%) and adropin (127 ± 106%) increased (p ≤ .0.05) only after DSW. Significant (p ≤ 0.01) partial correlations were found between the pre- to post-DSW changes in C1q, apelin or adropin and changes in outcome measures [e.g., C1q and MVIC (r = - 0.837), apelin and SBP (r = - 0.854), and andropin and OGTT (r = - 0.729)]. These results showed that greater decreases in plasma C1q and greater increases in apelin and adropin concentrations were associated with greater improvements in outcome measures after DSW than after ASW.
3. The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster
C Samakovlis, P Kylsten, D A Kimbrell, A Engström, D Hultmark EMBO J. 1991 Jan;10(1):163-9. doi: 10.1002/j.1460-2075.1991.tb07932.x.
In our study of the cecropin locus in Drosophila we have found a gene for a new peptide, andropin, with antibacterial properties. Transcripts from this gene, Anp, could be detected in newly eclosed males and reached steady-state levels after 1 day. Transcription was strongly induced in response to mating and is strictly confined to the ejaculatory duct of adult males. The deduced peptide sequence reveals a hydrophobic amino terminus with striking similarity to the signal peptide of the cecropins. The sequence of the predicted mature andropin shows no direct homology with the cecropins, but the two peptides may have similar secondary structures. We have synthesized the predicted gene product and shown it to be antibacterial. Crude extracts from male genital tracts show a potent bactericidal activity, and electrophoretic separation revealed at least three antibacterial components, one with the same mobility as the synthetic peptide. It appears that insects have evolved a mechanism for the protection of the seminal fluid and the male reproductive tract against microbial infections.
Online Inquiry
Verification code
Inquiry Basket