A peptide fragment of amylin
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Amylin (8-37) (human) (trifluoroacetate salt)

Item No. 24894

Technical Information
Formal Name
L-alanyl-L-threonyl-L-glutaminyl-L-arginyl-L-leucyl-L-alanyl-L-asparaginyl-L-phenylalanyl-L-leucyl-L-valyl-L-histidyl-L-seryl-L-seryl-L-asparaginyl-L-asparaginyl-L-phenylalanylglycyl-L-alanyl-L-isoleucyl-L-leucyl-L-seryl-L-seryl-L-threonyl-L-asparaginyl-L-valylglycyl-L-seryl-L-asparaginyl-L-threonyl-L-tyrosine, trifluoroacetate salt
Synonyms
  • IAPP (8-37) (human)
  • Islet Amyloid Polypeptide (8-37) (human)
Molecular Formula
C138H215N41O46 • XCF3COOH
Formula Weight
Purity
≥95%
A lyophilized powder
Water: 1 mg/ml
SMILES
[H]N[C@H](C(N[C@]([C@@H](C)O)([H])C(N[C@@H](CCC(N)=O)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(C)C)C(N[C@H](C(N[C@@H](CC(N)=O)C(N[C@H](C(N[C@@H](CC(C)C)C(N[C@@H](C(C)C)C(N[C@H](C(N[C@@H](CO)C(N[C@@H](CO)C(N[C@@H](CC(N)=O)C(N[C@@H](CC(N)=O)C(N[C@H](C(NCC(N[C@H](C(N[C@]([C@H](CC)C)([H])C(N[C@@H](CC(C)C)C(N[C@@H](CO)C(N[C@@H](CO)C(N[C@]([C@@H](C)O)([H])C(N[C@@H](CC(N)=O)C(N[C@@H](C(C)C)C(NCC(N[C@@H](CO)C(N[C@@H](CC(N)=O)C(N[C@]([C@@H](C)O)([H])C(N[C@H](C(O)=O)CC1=CC=C(O)C=C1)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)C)=O)=O)CC2=CC=CC=C2)=O)=O)=O)=O)=O)CC3=CN=CN3)=O)=O)=O)CC4=CC=CC=C4)=O)=O)C)=O)=O)=O)=O)=O)C.FC(F)(C(O)=O)F
InChi Code
InChI=1S/C138H215N41O46.C2HF3O2/c1-19-65(12)106(133(220)166-80(40-61(4)5)117(204)170-93(56-182)129(216)173-95(58-184)130(217)179-108(70(17)186)135(222)168-89(50-101(145)194)124(211)174-104(63(8)9)131(218)151-53-103(196)155-91(54-180)126(213)165-88(49-100(144)193)125(212)178-109(71(18)187)136(223)169-90(137(224)225)44-74-32-34-76(188)35-33-74)176-112(199)67(14)153-102(195)52-150-113(200)82(42-72-27-22-20-23-28-72)161-121(208)86(47-98(142)191)163-122(209)87(48-99(143)192)164-127(214)92(55-181)172-128(215)94(57-183)171-119(206)84(45-75-51-148-59-152-75)167-132(219)105(64(10)11)175-123(210)81(41-62(6)7)160-118(205)83(43-73-29-24-21-25-30-73)162-120(207)85(46-97(141)190)158-111(198)68(15)154-116(203)79(39-60(2)3)159-114(201)77(31-26-38-149-138(146)147)156-115(202)78(36-37-96(140)189)157-134(221)107(69(16)185)177-110(197)66(13)139;3-2(4,5)1(6)7/h20-25,27-30,32-35,51,59-71,77-95,104-109,180-188H,19,26,31,36-50,52-58,139H2,1-18H3,(H2,140,189)(H2,141,190)(H2,142,191)(H2,143,192)(H2,144,193)(H2,145,194)(H,148,152)(H,150,200)(H,151,218)(H,153,195)(H,154,203)(H,155,196)(H,156,202)(H,157,221)(H,158,198)(H,159,201)(H,160,205)(H,161,208)(H,162,207)(H,163,209)(H,164,214)(H,165,213)(H,166,220)(H,167,219)(H,168,222)(H,169,223)(H,170,204)(H,171,206)(H,172,215)(H,173,216)(H,174,211)(H,175,210)(H,176,199)(H,177,197)(H,178,212)(H,179,217)(H,224,225)(H4,146,147,149);(H,6,7)/t65-,66-,67-,68-,69+,70+,71+,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,104-,105-,106-,107-,108-,109-;/m0./s1
InChi Key
LEJOSZKCTLTERK-OJNSZWJJSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    Product Description

    Amylin (8-37) is a peptide fragment of amylin (Item Nos. 24274 | 24275).1 It inhibits osteoblast proliferation, but not bone resorption, induced by full-length human amylin and does not act as an agonist at amylin receptors. Amylin (8-37) induces formation of polymorphic fibrils containing coiled and laterally-associated sheet structures.2 It is cytotoxic to RINm5F islet β-cells in vitro when used at a concentration of 25 µM, an effect that is inversely correlated with mature fibril content.3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Cornish, J., Callon, K.E., Lin, C.Q., et alDissociation of the effects of amylin on osteoblast proliferation and bone resorption. Am. J. Physiol. 274(5 Pt 1), E827-833 (1998).

    2. Goldsbury, C., Goldie, K., Pellaud, J., et alAmyloid fibril formation from full-length and fragments of amylin. J. Struct. Biol. 130(2-3), 352-362 (2000).

    3. Konarkowska, B., Aitken, J.F., Kistler, J., et alThe aggregation potential of human amylin determines its cytotoxicity towards islet β-cells. FEBS J. 273(15), 3614-3624 (2006).