A neuropeptide with diverse biological activities
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Bombesin (trifluoroacetate salt)

Item No. 24151

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
5-oxo-L-prolyl-L-glutaminyl-L-arginyl-L-leucylglycyl-L-asparaginyl-L-glutaminyl-L-tryptophyl-L-alanyl-L-valylglycyl-L-histidyl-L-leucyl-L-methioninamide, trifluoroacetate salt
Synonyms
  • Glp-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
Molecular Formula
C71H110N24O18S • XCF3COOH
Formula Weight
1619.9
Purity
≥95%
Formulation (Request formulation change)
A lyophilized powder
Solubility(Learn about Variance in Solubility)
Water: 1 mg/ml
SMILES
O=C(N[C@H](C(N[C@@H](C(C)C)C(NCC(N[C@H](C(N[C@@H](CC(C)C)C(N[C@H](C(N)=O)CCSC)=O)=O)CC1=CN=CN1)=O)=O)=O)C)[C@@H](NC([C@H](CCC(N)=O)NC([C@H](CC(N)=O)NC(CNC([C@@H](NC([C@H](CCCNC(N)=N)NC([C@@H](NC([C@@H]2CCC(N2)=O)=O)CCC(N)=O)=O)=O)CC(C)C)=O)=O)=O)=O)CC3=CNC4=C3C=CC=C4.OC(C(F)(F)F)=O
InChi Code
InChI=1S/C71H110N24O18S.C2HF3O2/c1-34(2)24-47(92-62(105)43(14-11-22-79-71(76)77)89-64(107)45(15-18-52(72)96)90-63(106)44-17-20-55(99)85-44)61(104)81-31-56(100)87-51(28-54(74)98)69(112)91-46(16-19-53(73)97)65(108)94-49(26-38-29-80-41-13-10-9-12-40(38)41)66(109)84-37(7)60(103)95-58(36(5)6)70(113)82-32-57(101)86-50(27-39-30-78-33-83-39)68(111)93-48(25-35(3)4)67(110)88-42(59(75)102)21-23-114-8;3-2(4,5)1(6)7/h9-10,12-13,29-30,33-37,42-51,58,80H,11,14-28,31-32H2,1-8H3,(H2,72,96)(H2,73,97)(H2,74,98)(H2,75,102)(H,78,83)(H,81,104)(H,82,113)(H,84,109)(H,85,99)(H,86,101)(H,87,100)(H,88,110)(H,89,107)(H,90,106)(H,91,112)(H,92,105)(H,93,111)(H,94,108)(H,95,103)(H4,76,77,79);(H,6,7)/t37-,42-,43-,44-,45-,46-,47-,48-,49-,50-,51-,58-;/m0./s1
InChi Key
QTJOWWFKAATEOQ-ATNPYGLASA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    500 µg

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    1 mg

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    Product Description

    Bombesin is a neuropeptide with diverse biological activities originally isolated from the skin of B. bombina and B. variegata variegata amphibians.1,2 It binds to the gastrin-releasing peptide receptor (GRPR) in rat pancreatic acinar cells (Ki = 1.88 nM) and to frog bombesin receptor subtype 4 (BB4) in CHO cells overexpressing the receptor (Ki = 1.7 nM).3 Hypothalamic paraventricular microinfusion of bombesin (100 ng per animal) increases blood glucose, free fatty acids, and corticosterone levels in rats.4 Bombesin (50 ng per animal) injection into the preoptic area decreases food intake by food-deprived or insulin pretreated rats.5 It delays gastric emptying in rats by 55.8% when administered at a dose of 16 μg/kg (i.p.) and inhibits gastric secretion at a dose of 500 ng per animal.6,7

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Anastasi, A., Erspamer, V., and Bucci, M. Isolation and structure of bombesin and alytesin, two analogous active peptides from the skin of the European amphibians Bombina and Alytes. Experientia 27(2), 166-167 (1971).

    2. Weber, H.C. Regulation and signaling of human bombesin receptors and their biological effects. Curr. Opin. Endocrinol. Diabetes Obes. 16(1), 66-71 (2009).

    3. Pradhan, T.K., Katsuno, T., Taylor, J.E., et al. Identification of a unique ligand which has high affinity for all four bombesin receptor subtypes. Eur. J. Pharmacol. 343(2-3), 275-287 (1998).

    4. Gunion, M.W., Taché, Y., Rosenthal, M.J., et al. Bombesin microinfusion into the rat hypothalamic paraventricular nucleus increases blood glucose, free fatty acids and corticosterone. Brain Res. 478(1), 47-58 (1989).

    5. Babcock, A.M., Barton, C., Gunion, M.W., et al. Bombesin-induced hypothermia and hypophagia are associated with plasma metabolic fuel alterations in the rat. Physiol. Behav. 51(5), 933-938 (1992).

    6. Scarpignato, C., and Bertaccini, G. Bombesin delays gastric emptying in the rat. Digestion 21(2), 104-106 (1981).

    7. Tache, Y., Lesiege, D., and Goto, Y. Neural pathways involved in intracisternal bombesin-induced inhibition of gastric secretion in rats. Dig. Dis. Sci. 31(4), 412-417 (1986).