Recombinant Major Royal Jelly protein 1 (His tag)
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Recombinant Major Royal Jelly protein 1 (His tag) is a Apis mellifera Full Length protein, in the 20 to 432 aa range, expressed in Yeast, with >90%, suitable for SDS-PAGE.
View Alternative Names
GB14888, MRJP1, Major royal jelly protein 1, 56-kDa protein 4, Apalbumin 1, Apisin subunit MRJP1, Bee-milk protein, Royal jelly protein RJP57-3, Royalactin, p56kP-4, RJP-3
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Major Royal Jelly protein 1 (His tag) (AB241437)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab241437.
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Form
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MRJP1 plays an essential role in the development and growth of bee larvae. It is part of a larger protein complex that influences the differentiation between worker and queen bees. The protein has immunomodulatory and antioxidant properties contributing to the overall health and longevity of the queen bee. MRJP1's glycoprotein nature also helps it bind with other molecules which affects honeybee nutrition and development significantly.
Pathways
MRJP1 participates in the insulin/IGF-like signaling pathway. This pathway plays a significant role in growth regulation making it essential for the development of the queen bee. MRJP1 also interacts with the TOR pathway which is involved in protein synthesis and cell growth. This interaction makes MRJP1 related to proteins like IGFR and TOR which are necessary for normal metabolic and growth functions within honeybee physiology.
General info
Function
Major royal jelly protein 1. Most abundant protein component of royal jelly, a substance produced in the hypopharyngeal gland containing proteins, free amino acids, fatty acids, sugars and other nutrients, which is fed to developing larvae by worker nurse bees (PubMed : 15607658, PubMed : 20017154, PubMed : 21516106, PubMed : 31410279, PubMed : 9791542). Major royal jelly proteins (Mrjps) are high in essential amino acids and probably have a nutritional function in larval food (PubMed : 9791542). All larvae are fed some royal jelly (also known as worker jelly) early in their development but it forms the principal source of nutrition for larvae destined to become queen bees (Probable). Induces the differentiation of honey bee larvae into queens through an Egfr-mediated signaling pathway (PubMed : 21516106). Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing 20-hydroxyecdysone (ecdysterone, 20E) production (PubMed : 21516106). Together with apisimin forms the apisin complex that polymerizes at low pH, forming a fiber network and increasing the viscosity of royal jelly (PubMed : 29551410). The viscous royal Jelly placed in honeycomb cells containing larvae destined to become queens acts as both a food supply and an adhesive preventing larvae from falling out; queens are reared in special large cells oriented vertically (PubMed : 29551410). Produced in the spermatheca of adult queen bees, along with other major royal jelly proteins, where it may act as a nutrient supply for sperm stored by mated queens, or be involved in energy metabolism (PubMed : 34442256). In the brain, involved in determining worker bee behavior and the transition from nursing to foraging; high levels of Mrjp1 and Mrjp3 promote nursing behavior (PubMed : 36414079).. Jellein-1. Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans (PubMed : 15203237, PubMed : 31862270). Has antiparasitic activity against Leishmania major, inhibiting proliferation at the promastigote stage but not the amastigote stage; alters membrane permeability and membrane potential of promastigote cells (PubMed : 31862270). Lacks significant cytolytic activity and does not induce rat peritoneal mast cell degranulation (PubMed : 15203237). Has very low hemolytic activity (PubMed : 31862270).. Jellein-2. Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation.. Jellein-4. Lacks antibacterial and antifungal activity. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation.
Sequence similarities
Belongs to the major royal jelly protein family.
Post-translational modifications
N-glycosylated on Asn-28, Asn-144 and Asn-177 (PubMed:30135511, PubMed:33293513, PubMed:9395329). Glycosylation is required to prevent apisin multimers from aggregating (PubMed:28252287).. Jellein-2 is probably processed to yield jellein-1 and jellein-4.
Subcellular localisation
Cytoskeleton
Target data
Product promise
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