Human Islet Amyloid Polypeptide (IAPP) Peptide (OVA)

494€ (100 µg)
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935106861
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name
Human Islet Amyloid Polypeptide (IAPP) Peptide (OVA)
category
Proteins and Peptides
provider
Abbexa
reference
abx651025
tested applications
WB, SDS-PAGE
Description
Islet Amyloid Polypeptide Protein (OVA) is a Human protein conjugated to OVA.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Islet Amyloid Polypeptide (IAPP) |
| Host | Synthetic |
| Assay Type | Activity: Not tested Sequence Fragment: Asn36-Leu60 |
| Origin | Human |
| Conjugation | OVA |
| Expression | Synthetic |
| Purity | > 90% |
| Size 1 | 100 µg |
| Size 2 | 200 µg |
| Size 3 | 500 µg |
| Size 4 | 1 mg |
| Size 5 | 5 mg |
| Form | Lyophilized |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles. |
| Dry Ice | No |
| Alias | Amylin,IAP,Diabetes-Associated Peptide Diabetes-Associated Peptide |
| Background | Protein IAPP |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. Concentration: Prior to lyophilization: 200 µg/ml |
Descripción
Islet amyloid polypeptide (IAPP), also known as amylin, is a 37-residue peptide hormone produced by the pancreatic beta cells. IAPP plays a role in regulating glucose metabolism, primarily by slowing gastric emptying and reducing glucagon secretion. in conditions such as type 2 diabetes mellitus, IAPP can misfold and aggregate, forming amyloid fibrils. These amyloid fibrils can accumulate in the pancreas, particularly in the islets of Langerhans. This aggregation of amyloid fibrils is associated with beta cell dysfunction, apoptosis , and progression of type 2 diabetes. Amyloid deposits originating from islet amyloid polypeptide (IAPP), are frequently observed in the pancreatic islets of individuals with type 2 diabetes mellitus or those afflicted with insulinoma cancer. Although the connection between amylin and the onset of type 2 diabetes has been recognized for some time, pinpointing its direct causative role has proved challenging. Some research indicates that amylin, and beta-amyloid (Abeta) linked to Alzheimer's disease, could trigger apoptotic cell death in insulin-producing beta cells. This effect may have implications for the progression of type 2 diabetes.
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