Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
Description
About Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
Amylin (1-37) is a peptide hormone co-secreted with insulin by the pancreas and contributes to glycemic control. Other names are: amlintide, amylin (1 - 37), amylin, pancreatic amylin, islet amyloid, islet amyloid polypeptide precursor, IAPP precursor. Amylin is able to form amyloid fibers and composes protein deposits in the Islets of Langerhans of patients with noninsulin-dependent diabetes mellitus. For research use only, do not use in humans!
Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human - Specifications
- Peptide sequence: H-KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2, Disulfide
- Amount: 1.0 mg net (AAA)
- Purity: >95% (HPLC-MS)
- Counterion: TFA
- Delivery Format: Freeze-dried in plastic vial
- Chemical formula: C165H261N51O55S2
- MW (average): 3903.33
- Application(s): Diabetes research
- Condition(s)/Topic(s): Diabetes
- Standard Delivery Time: 2-5 days
- CAS: 122384-88-7
- SMILES: O=C(N[C@H](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)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CC(C)C)C(N[C@@H](CO)C(N[C@@H](CO)C(N[C@@H]([C@@H](C)O)C(N[C@@H](CC(N)=O)C(N[C@@H](C(C)C)C(NCC(N[C@@H](CO)C(N[C@H](C(N[C@H](C(N[C@H](C(N)=O)CC1=CC=C(O)C=C1)=O)[C@H](O)C)=O)CC(N)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)CC2=CC=CC=C2)=O)=O)=O)=O)CO)[C@H](CC3=CNC=N3)NC([C@H](C(C)C)NC([C@H](CC(C)C)NC([C@H](CC4=CC=CC=C4)NC([C@H](CC(N)=O)NC([C@H](C)NC([C@H](CC(C)C)NC([C@H](CCCNC(N)=N)NC([C@H](CCC(N)=O)NC([C@H]([C@@H](C)O)NC([C@H](C)NC([C@H]5NC([C@H]([C@H](O)C)NC([C@H](C)NC([C@H]([C@H](O)C)NC([C@H](CC(N)=O)NC([C@H](CSSC5)NC([C@H](N)CCCCN)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O
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JPT’s Amylin Peptides
Amylin 1-37 (or Islet Amyloid Polypeptide, IAPP) is a peptide hormone with the primary sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY. The C-terminus is amidated and it contains a disulfide bridge (2-7) which is necessary for the full biological activity of amylin. Amylin and insulin are co-secreted from pancreatic β-cells. Amylin inhibits glucagon secretion and delays gastric emptying, thus acting as a satiety agent. Amylin can form fibrillar peptide deposits in the islets of Langerhans, which may be related to death of the insulin-producing islet cells in type 2 diabetes. Amylin is also expressed in the human placenta during pregnancy. JPT Peptide Technologies has substantial, long-standing expertise in providing peptides in all formats, scales and modifications to the global scientific community. All our catalog peptides are provided with HPLC-MS analyses to confirm the identity and demonstrate the high quality of our peptides.
Benefits of JPT’s Peptides- All peptides are made in Germany
- Bulk orders or custom peptide synthesis upon request
- Provision of freeze-dried aliquots for enhanced stability
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References
References for Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
References:
Read References with Specialty Peptides
Testimonial:
"Our group focuses on the in vitro study of risk factors in Alzheimer’s disease and, as we experienced that the in-house expression and production of the amyloid beta peptide is notoriously difficult, we are continuously dependent on a high quality supply of a large variety of these peptides from commercial source.We started our collaboration with JPT with their request to test a range of their peptides for the ability to produce toxic oligomers and fibrillar networks and were impressed by the rapid supply of a very wide range of high purity peptides with excellent fibril forming properties and toxicity profiles. JPT has shown real valuable know-how and experience in the field of peptide synthesis by their ability to generate high quality preparations of amyloid beta peptide variants which are known for their difficulty to handle."
Kerensa Broersen, Assistant Prof., Nanobiophysics Group, University of Twente, Enschede, The Netherlands
Testimonial:
Our group focuses on the in vitro study of risk factors in Alzheimer’s disease and, as we experienced that the in-house expression and production of the amyloid beta peptide is notoriously difficult, we are continuously dependent on a high quality supply of a large variety of these peptides from commercial source.We started our collaboration with JPT with their request to test a range of their peptides for the ability to produce toxic oligomers and fibrillar networks and were impressed by the rapid supply of a very wide range of high purity peptides with excellent fibril forming properties and toxicity profiles. JPT has shown real valuable know-how and experience in the field of peptide synthesis by their ability to generate high quality preparations of amyloid beta peptide variants which are known for their difficulty to handle.
Kerensa Broersen, Assistant Prof., Nanobiophysics Group, University of Twente, Enschede, The Netherlands
Documentation
Documentation for Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
Properties
Properties of Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
Properties | Values |
---|---|
Amount: | 1.0 mg net (AAA) |
Application: | Diabetes research |
Category: | Diabetes Peptides |
Condition / Topic: | Diabetes |
Layout: | Freeze-dried in plastic vial |
Organism: | Human |
Protein Name: | Diabetes Peptide |
Purity: | >95% (HPLC-MS) |
Quantification: | Yes |
Further Information to Amylin (1-37), Islet Amyloid Polypeptide, IAPP, Human
Information | Values |
---|---|
Sequence: | H-KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2, Disulfide |