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Islet amyloid polypeptide (Amylin) (Diabetes-associated peptide) (DAP) (Insulinoma amyloid peptide)

 IAPP_HUMAN              Reviewed;          89 AA.
P10997; Q0ZD87; Q14598;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 175.
RecName: Full=Islet amyloid polypeptide;
AltName: Full=Amylin;
AltName: Full=Diabetes-associated peptide;
Short=DAP;
AltName: Full=Insulinoma amyloid peptide;
Flags: Precursor;
Name=IAPP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND AMIDATION AT TYR-70.
PubMed=2651160; DOI=10.1016/0014-5793(89)81260-8;
Mosselman S., Hoeppener J.W.M., Lips C.J.M., Jansz H.S.;
"The complete islet amyloid polypeptide precursor is encoded by two
exons.";
FEBS Lett. 247:154-158(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2608057; DOI=10.1210/mend-3-11-1775;
Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G.,
Shows T.B., Bell G.I., Steiner D.F.;
"Human islet amyloid polypeptide gene: complete nucleotide sequence,
chromosomal localization, and evolutionary history.";
Mol. Endocrinol. 3:1775-1781(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=3053705;
Sanke T., Bell G.I., Sample C., Rubenstein A.H., Steiner D.F.;
"An islet amyloid peptide is derived from an 89-amino acid precursor
by proteolytic processing.";
J. Biol. Chem. 263:17243-17246(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2365085; DOI=10.1016/0014-5793(90)80314-9;
Christmanson L., Rorsman F., Stenman G., Westermark P., Betsholtz C.;
"The human islet amyloid polypeptide (IAPP) gene. Organization,
chromosomal localization and functional identification of a promoter
region.";
FEBS Lett. 267:160-166(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2223885; DOI=10.1016/0167-4781(90)90210-S;
van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J.,
van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.;
"Islet amyloid polypeptide: structure and upstream sequences of the
IAPP gene in rat and man.";
Biochim. Biophys. Acta 1087:235-240(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1282806; DOI=10.1016/0006-291X(92)90255-J;
Hoeppener J.W.M., Oosterwijk C., Visser-Vernooy H.J., Lips C.J.M.,
Jansz H.S.;
"Characterization of the human islet amyloid polypeptide/amylin gene
transcripts: identification of a new polyadenylation site.";
Biochem. Biophys. Res. Commun. 189:1569-1577(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DOMAIN, AND MASS
SPECTROMETRY.
TISSUE=Fetal pancreas;
PubMed=17374526; DOI=10.1016/j.bbrc.2007.03.016;
Bhattacharya S., Naveena Lavanya Latha J., Kumresan R., Singh S.;
"Cloning and expression of human islet amyloid polypeptide in cultured
cells.";
Biochem. Biophys. Res. Commun. 356:622-628(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-89.
PubMed=3181427; DOI=10.1016/0014-5793(88)80922-0;
Mosselman S., Hoeppener J.W.M., Zandberg J., van Mansfeld A.D.M.,
Geurts van Kessel A.H.M., Lips C.J.M., Jansz H.S.;
"Islet amyloid polypeptide: identification and chromosomal
localization of the human gene.";
FEBS Lett. 239:227-232(1988).
[10]
PROTEIN SEQUENCE OF 34-70, AND DISULFIDE BOND.
PubMed=3317417; DOI=10.1073/pnas.84.23.8628;
Cooper G.J., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.;
"Purification and characterization of a peptide from amyloid-rich
pancreases of type 2 diabetic patients.";
Proc. Natl. Acad. Sci. U.S.A. 84:8628-8632(1987).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-70, AND SYNTHESIS OF 53-62.
PubMed=2666169; DOI=10.1016/0014-5793(89)81467-X;
Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V.,
Johnson K.H., Westermark P.;
"Sequence divergence in a specific region of islet amyloid polypeptide
(IAPP) explains differences in islet amyloid formation between
species.";
FEBS Lett. 251:261-264(1989).
[12]
PROTEIN SEQUENCE OF 34-70.
PubMed=2091067; DOI=10.1016/0167-0115(90)90004-G;
Nakazato M., Asai J., Miyazato M., Matsukura S., Kangawa K.,
Matsuo H.;
"Isolation and identification of islet amyloid polypeptide in normal
human pancreas.";
Regul. Pept. 31:179-186(1990).
[13]
PROTEIN SEQUENCE OF 34-52.
PubMed=3535798; DOI=10.1016/0006-291X(86)90708-4;
Westermark P., Wernstedt C., Wilander E., Sletten K.;
"A novel peptide in the calcitonin gene related peptide family as an
amyloid fibril protein in the endocrine pancreas.";
Biochem. Biophys. Res. Commun. 140:827-831(1986).
[14]
PROTEIN SEQUENCE OF 34-70.
PubMed=3035556; DOI=10.1073/pnas.84.11.3881;
Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D.,
Johnson K.H.;
"Amyloid fibrils in human insulinoma and islets of Langerhans of the
diabetic cat are derived from a neuropeptide-like protein also present
in normal islet cells.";
Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987).
[15]
PROTEIN SEQUENCE OF 30-89.
PubMed=2690069; DOI=10.1073/pnas.86.24.9662;
Roberts A.N., Leighton B., Todd J.A., Cockburn D., Schofield P.N.,
Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C.,
Reid K.B.M., Cooper G.J.S.;
"Molecular and functional characterization of amylin, a peptide
associated with type 2 diabetes mellitus.";
Proc. Natl. Acad. Sci. U.S.A. 86:9662-9666(1989).
[16]
STRUCTURE BY NMR OF IAPP.
PubMed=2039456; DOI=10.1042/bj2750785;
Hubbard J.A.M., Martin S.R., Chaplin L.C., Bose C., Kelly S.M.,
Price N.C.;
"Solution structures of calcitonin-gene-related-peptide analogues of
calcitonin-gene-related peptide and amylin.";
Biochem. J. 275:785-788(1991).
[17]
STRUCTURE BY NMR OF 53-62 IN DETERGENT MICELLES.
PubMed=12717720; DOI=10.1002/bip.10305;
Mascioni A., Porcelli F., Ilangovan U., Ramamoorthy A., Veglia G.;
"Conformational preferences of the amylin nucleation site in SDS
micelles: an NMR study.";
Biopolymers 69:29-41(2003).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 34-70 IN COMPLEX WITH IDE,
AND INTERACTION WITH IDE.
PubMed=17051221; DOI=10.1038/nature05143;
Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.;
"Structures of human insulin-degrading enzyme reveal a new substrate
recognition mechanism.";
Nature 443:870-874(2006).
[19]
STRUCTURE BY NMR OF 34-70 IN DETERGENT MICELLES, DOMAIN, AND DISULFIDE
BOND.
PubMed=19244249; DOI=10.1074/jbc.M809085200;
Patil S.M., Xu S., Sheftic S.R., Alexandrescu A.T.;
"Dynamic alpha-helix structure of micelle-bound human amylin.";
J. Biol. Chem. 284:11982-11991(2009).
[20]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH INS, DISULFIDE
BOND, MUTAGENESIS OF PHE-48, AND DOMAIN.
PubMed=19475663; DOI=10.1002/pro.145;
Wiltzius J.J., Sievers S.A., Sawaya M.R., Eisenberg D.;
"Atomic structures of IAPP (amylin) fusions suggest a mechanism for
fibrillation and the role of insulin in the process.";
Protein Sci. 18:1521-1530(2009).
[21]
VARIANT GLY-53.
PubMed=8772735; DOI=10.2337/diab.45.9.1279;
Sakagashira S., Sanke T., Hanabusa T., Shimomura H., Ohagi S.,
Kumagaye K.Y., Nakajima K., Nanjo K.;
"Missense mutation of amylin gene (S20G) in Japanese NIDDM patients.";
Diabetes 45:1279-1281(1996).
[22]
VARIANT GLY-53.
PubMed=9794116; DOI=10.1007/s001250051060;
Chuang L.M., Lee K.C., Huang C.N., Wu H.P., Tai T.Y., Lin B.J.;
"Role of S20G mutation of amylin gene in insulin secretion, insulin
sensitivity, and type II diabetes mellitus in Taiwanese patients.";
Diabetologia 41:1250-1251(1998).
-!- FUNCTION: Selectively inhibits insulin-stimulated glucose
utilization and glycogen deposition in muscle, while not affecting
adipocyte glucose metabolism.
-!- SUBUNIT: Interacts with IDE and INS. Can form homodimers.
Interaction with INS inhibits homodimerization and fibril
formation. {ECO:0000269|PubMed:17051221,
ECO:0000269|PubMed:19475663}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-8526679, EBI-8526679;
P14735-1:IDE; NbExp=3; IntAct=EBI-8526679, EBI-15607031;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17374526}.
-!- DOMAIN: The mature protein is largely unstructured in the absence
of a cognate ligand, and has a strong tendency to form fibrillar
aggregates. Homodimerization may be the first step of amyloid
formation. {ECO:0000269|PubMed:17374526,
ECO:0000269|PubMed:19244249, ECO:0000269|PubMed:19475663}.
-!- PTM: Amyloid fibrils are degraded by IDE.
-!- MASS SPECTROMETRY: Mass=3936; Method=MALDI; Range=34-70;
Evidence={ECO:0000269|PubMed:17374526};
-!- MISCELLANEOUS: IAPP is the peptide subunit of amyloid found in
pancreatic islets of type 2 diabetic patients and in insulinomas.
-!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Amylin entry;
URL="https://en.wikipedia.org/wiki/Amylin";
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EMBL; M27503; AAA35524.1; -; Genomic_DNA.
EMBL; X14904; CAA33032.1; -; mRNA.
EMBL; X14905; CAA33033.1; -; mRNA.
EMBL; X14902; CAA33031.1; -; Genomic_DNA.
EMBL; X14903; CAB57804.1; -; Genomic_DNA.
EMBL; X13859; CAB57803.1; -; Genomic_DNA.
EMBL; J04422; AAA52281.1; -; mRNA.
EMBL; M21785; AAA51728.1; -; Genomic_DNA.
EMBL; M26650; AAA35983.1; -; Genomic_DNA.
EMBL; X52818; CAA37002.1; -; Genomic_DNA.
EMBL; X52819; CAA37002.1; JOINED; Genomic_DNA.
EMBL; X56030; CAA39504.1; -; Genomic_DNA.
EMBL; X55634; CAA39504.1; JOINED; Genomic_DNA.
EMBL; X68830; CAA48724.1; -; Genomic_DNA.
EMBL; DQ516082; ABG27010.1; -; mRNA.
EMBL; CH471094; EAW96426.1; -; Genomic_DNA.
CCDS; CCDS8688.1; -.
PIR; S04016; TCHUIA.
RefSeq; NP_000406.1; NM_000415.2.
RefSeq; NP_001316130.1; NM_001329201.1.
UniGene; Hs.46835; -.
PDB; 1KUW; NMR; -; A=53-62.
PDB; 2G48; X-ray; 2.60 A; C/D=34-70.
PDB; 2KB8; NMR; -; A=34-70.
PDB; 2L86; NMR; -; A=34-70.
PDB; 3DG1; X-ray; 1.66 A; A=61-66.
PDB; 3FPO; X-ray; 1.50 A; A=51-56.
PDB; 3FR1; X-ray; 1.85 A; A=47-52.
PDB; 3FTH; X-ray; 1.84 A; A/B=47-53.
PDB; 3FTK; X-ray; 1.50 A; A=64-70.
PDB; 3FTL; X-ray; 1.60 A; A/B=64-70.
PDB; 3FTR; X-ray; 1.61 A; A=61-66.
PDB; 3G7V; X-ray; 1.86 A; A/B/C/D=34-69.
PDB; 3G7W; X-ray; 1.75 A; A=34-55.
PDB; 3HGZ; X-ray; 2.91 A; D/E=34-70.
PDB; 5K5G; NMR; -; A=34-70.
PDB; 5KNZ; EM; 1.90 A; A=52-62.
PDB; 5KO0; EM; 1.40 A; A/B=48-58.
PDB; 5MGQ; NMR; -; A=34-69.
PDBsum; 1KUW; -.
PDBsum; 2G48; -.
PDBsum; 2KB8; -.
PDBsum; 2L86; -.
PDBsum; 3DG1; -.
PDBsum; 3FPO; -.
PDBsum; 3FR1; -.
PDBsum; 3FTH; -.
PDBsum; 3FTK; -.
PDBsum; 3FTL; -.
PDBsum; 3FTR; -.
PDBsum; 3G7V; -.
PDBsum; 3G7W; -.
PDBsum; 3HGZ; -.
PDBsum; 5K5G; -.
PDBsum; 5KNZ; -.
PDBsum; 5KO0; -.
PDBsum; 5MGQ; -.
ProteinModelPortal; P10997; -.
SMR; P10997; -.
BioGrid; 109604; 1.
DIP; DIP-29913N; -.
IntAct; P10997; 1.
MINT; MINT-8074874; -.
STRING; 9606.ENSP00000240652; -.
ChEMBL; CHEMBL1914266; -.
iPTMnet; P10997; -.
PhosphoSitePlus; P10997; -.
BioMuta; IAPP; -.
DMDM; 124006; -.
PaxDb; P10997; -.
PeptideAtlas; P10997; -.
PRIDE; P10997; -.
DNASU; 3375; -.
Ensembl; ENST00000240652; ENSP00000240652; ENSG00000121351.
Ensembl; ENST00000539393; ENSP00000437357; ENSG00000121351.
GeneID; 3375; -.
KEGG; hsa:3375; -.
UCSC; uc001rev.4; human.
CTD; 3375; -.
DisGeNET; 3375; -.
EuPathDB; HostDB:ENSG00000121351.7; -.
GeneCards; IAPP; -.
HGNC; HGNC:5329; IAPP.
HPA; CAB000352; -.
HPA; HPA053194; -.
MIM; 147940; gene.
neXtProt; NX_P10997; -.
OpenTargets; ENSG00000121351; -.
PharmGKB; PA29579; -.
eggNOG; ENOG410J0NB; Eukaryota.
eggNOG; ENOG410Z7V7; LUCA.
GeneTree; ENSGT00510000048671; -.
HOGENOM; HOG000038203; -.
HOVERGEN; HBG096065; -.
InParanoid; P10997; -.
KO; K08039; -.
OMA; SHQMEKR; -.
OrthoDB; EOG091G15QG; -.
PhylomeDB; P10997; -.
TreeFam; TF330783; -.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
Reactome; R-HSA-977225; Amyloid fiber formation.
EvolutionaryTrace; P10997; -.
GeneWiki; Amylin; -.
GenomeRNAi; 3375; -.
PMAP-CutDB; P10997; -.
PRO; PR:P10997; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000121351; -.
CleanEx; HS_IAPP; -.
ExpressionAtlas; P10997; baseline and differential.
Genevisible; P10997; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016234; C:inclusion body; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0097647; P:amylin receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:1990000; P:amyloid fibril formation; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; TAS:ARUK-UCL.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010823; P:negative regulation of mitochondrion organization; TAS:ARUK-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; TAS:ARUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:ARUK-UCL.
GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IGI:ARUK-UCL.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; IGI:ARUK-UCL.
GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; NAS:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; NAS:ARUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:ARUK-UCL.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; IGI:ARUK-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:ARUK-UCL.
GO; GO:0031648; P:protein destabilization; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR021117; Calcitonin-like.
InterPro; IPR021116; Calcitonin/adrenomedullin.
InterPro; IPR018360; Calcitonin_CS.
InterPro; IPR001693; Calcitonin_peptide-like.
InterPro; IPR000443; Pro-islet_amyloid_polypep.
PANTHER; PTHR10505; PTHR10505; 2.
PANTHER; PTHR10505:SF4; PTHR10505:SF4; 2.
Pfam; PF00214; Calc_CGRP_IAPP; 1.
PRINTS; PR00818; ISLETAMYLOID.
SMART; SM00113; CALCITONIN; 1.
PROSITE; PS00258; CALCITONIN; 1.
1: Evidence at protein level;
3D-structure; Amidation; Amyloid; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond; Hormone;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 31
/FTId=PRO_0000004105.
PEPTIDE 34 70 Islet amyloid polypeptide.
/FTId=PRO_0000004106.
PROPEP 74 89
/FTId=PRO_0000004107.
MOD_RES 70 70 Tyrosine amide.
{ECO:0000269|PubMed:2651160,
ECO:0000269|PubMed:3053705}.
DISULFID 35 40 {ECO:0000269|PubMed:19244249,
ECO:0000269|PubMed:19475663,
ECO:0000269|PubMed:3317417}.
VARIANT 53 53 S -> G (in dbSNP:rs1800203).
{ECO:0000269|PubMed:8772735,
ECO:0000269|PubMed:9794116}.
/FTId=VAR_012080.
MUTAGEN 48 48 F->A,D,S: Promotes formation of fibrillar
aggregates.
{ECO:0000269|PubMed:19475663}.
CONFLICT 53 53 S -> C (in Ref. 4; CAA39504).
{ECO:0000305}.
HELIX 36 38 {ECO:0000244|PDB:2G48}.
STRAND 45 47 {ECO:0000244|PDB:5K5G}.
STRAND 49 57 {ECO:0000244|PDB:5KO0}.
TURN 59 61 {ECO:0000244|PDB:1KUW}.
TURN 63 69 {ECO:0000244|PDB:2L86}.
SEQUENCE 89 AA; 9806 MW; AA8B1F7FD9FCB4BD CRC64;
MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV HSSNNFGAIL
SSTNVGSNTY GKRNAVEVLK REPLNYLPL


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06-271-83062 Amylin (8-37) Rat - Diabetes-associated peptide; DAP; Amylin; Insulinoma amyloid peptide 1 mg
H-5708.0001 Amylin (1_13) (human) Salt _ Binding (Disulfide_bond) Synonym Islet Amyloid Polypeptide (1_13) (human), DAP (1_13) (human), Insulinoma Amyloid Peptide (1_13) (human), Diabetes_Associated Peptide (1 1.0 mg
H-5708.0001 Amylin (1_13) (human) Salt _ Binding (Disulfide_bond) Synonym Islet Amyloid Polypeptide (1_13) (human), DAP (1_13) (human), Insulinoma Amyloid Peptide (1_13) (human), Diabetes_Associated Peptide (1 1.0 mg
18-272-196257 Amylin - Rabbit polyclonal to Amylin; Amylin; Diabetes-associated peptide; DAP; Insulinoma amyloid peptide Polyclonal 1 ml
20-272-190339 Amylin - Mouse monoclonal [ R10 _ 99 ] to Amylin; Amylin; Diabetes-associated peptide; DAP; Insulinoma amyloid peptide Monoclonal 1 ml
18-272-196258 Amylin prediluted - Rabbit polyclonal to Amylin prediluted; Amylin; Diabetes-associated peptide; DAP; Insulinoma amyloid peptide Polyclonal 7 ml
ICCB29-1 Amylin, Islet Amyloid Polypeptide (IAPP), Rabbit anti_ 50 µl.
E0036Hu Human pro-islet amyloid polypeptide-Pro-amylin,proIAPP ELISA Kit 96T


 

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