Bombinakinin-GAP

Bioactive, bradykinin-related peptide CAS# 573671-91-7

Bombinakinin-GAP

2D Structure

Catalog No. BCC5903----Order now to get a substantial discount!

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3D structure

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Bombinakinin-GAP

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Chemical Properties of Bombinakinin-GAP

Cas No. 573671-91-7 SDF Download SDF
PubChem ID 90473869 Appearance Powder
Formula C145H219N39O39S3 M.Wt 3228.75
Type of Compound N/A Storage Desiccate at -20°C
Synonyms Bombinakinin M Gene Associated Peptide
Solubility Soluble to 1 mg/ml in water
Sequence DMYEIKQYKTAHGRPPICAPGEQCPIWV

(Modifications: Val-28 = C-terminal amide, Disulfide bridge between 18 - 24)

SMILES CCC(C)C(C(=O)NC1CSSCC(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C2CCCN2C(=O)C(NC1=O)C)CCC(=O)O)CCC(=O)N)C(=O)N3CCCC3C(=O)NC(C(C)CC)C(=O)NC(CC4=CNC5=CC=CC=C54)C(=O)NC(C(C)C)C(=O)N)NC(=O)C6CCCN6C(=O)C7CCCN7C(=O)C(CCCNC(=N)N)NC(=O)CNC(=O)C(CC8=CNC=N8)NC(=O)C(C)NC(=O)C(C(C)O)NC(=O)C(CCCCN)NC(=O)C(CC9=CC=C(C=C9)O)NC(=O)C(CCC(=O)N)NC(=O)C(CCCCN)NC(=O)C(C(C)CC)NC(=O)C(CCC(=O)O)NC(=O)C(CC1=CC=C(C=C1)O)NC(=O)C(CCSC)NC(=O)C(CC(=O)O)N
Standard InChIKey WGYUZJQRZYPVMG-BFMDKFMESA-N
Standard InChI InChI=1S/C145H219N39O39S3/c1-13-74(6)115(177-129(208)94(47-51-112(194)195)168-131(210)98(62-81-38-42-85(187)43-39-81)172-127(206)95(52-60-224-12)164-121(200)87(148)65-113(196)197)137(216)169-89(29-18-20-53-146)123(202)166-92(44-48-107(149)188)125(204)171-97(61-80-36-40-84(186)41-37-80)130(209)165-90(30-19-21-54-147)128(207)180-118(79(11)185)140(219)160-77(9)120(199)170-100(64-83-67-154-72-159-83)122(201)157-68-110(191)163-96(31-22-55-155-145(152)153)142(221)184-59-26-35-106(184)144(223)183-58-25-34-105(183)136(215)179-117(76(8)15-3)139(218)174-101-70-225-226-71-102(175-126(205)93(45-49-108(150)189)167-124(203)91(46-50-111(192)193)162-109(190)69-158-134(213)103-32-23-56-181(103)141(220)78(10)161-133(101)212)143(222)182-57-24-33-104(182)135(214)178-116(75(7)14-2)138(217)173-99(132(211)176-114(73(4)5)119(151)198)63-82-66-156-88-28-17-16-27-86(82)88/h16-17,27-28,36-43,66-67,72-79,87,89-106,114-118,156,185-187H,13-15,18-26,29-35,44-65,68-71,146-148H2,1-12H3,(H2,149,188)(H2,150,189)(H2,151,198)(H,154,159)(H,157,201)(H,158,213)(H,160,219)(H,161,212)(H,162,190)(H,163,191)(H,164,200)(H,165,209)(H,166,202)(H,167,203)(H,168,210)(H,169,216)(H,170,199)(H,171,204)(H,172,206)(H,173,217)(H,174,218)(H,175,205)(H,176,211)(H,177,208)(H,178,214)(H,179,215)(H,180,207)(H,192,193)(H,194,195)(H,196,197)(H4,152,153,155)/t74-,75-,76-,77-,78-,79+,87-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,114-,115-,116-,117-,118-/m0/s1
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Biological Activity of Bombinakinin-GAP

DescriptionBioactive bradykinin-related peptide. Induces a 60% reduction in food intake following i.c.v. administration in rats.

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References on Bombinakinin-GAP

Bombinakinin M gene associated peptide, a novel bioactive peptide from skin secretions of the toad Bombina maxima.[Pubmed:12668203]

Peptides. 2003 Feb;24(2):199-204.

A novel 28-amino acid peptide, termed Bombinakinin-GAP, was purified and characterized from skin secretions of the toad Bombina maxima. Its primary structure was established as DMYEIKQYKTAHGRPPICAPGEQCPIWV-NH(2), in which two cysteines form a disulfide bond. A FASTA search of SWISS-PROT databank detected a 32% sequence identity between the sequences of the peptide and a segment of rat cocaine- and amphetamine-regulated transcript (CART). Intracerebroventricular (i.c.v.) administration of the peptide induced a significant decrease in food intake in rats, suggesting that it played a role in the control of feeding by brain. Analysis of its cDNA structure revealed that this peptide is coexpressed with bombinakinin M, a bradykinin-related peptide from the same toad. Bombinakinin-GAP appears to be the first example of a novel class of bioactive peptides from amphibian skin, which may be implicated in feeding behavior.

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