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Rabbit Anti-IAPP Recombinant Antibody (CBYC-A977) (CBMAB-A4460-YC)

Provided herein is a Rabbit monoclonal antibody against Human Islet Amyloid Polypeptide. The antibody can be used for immunoassay techniques, such as IHC-Fr, IHC-P.
See all IAPP antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Cat, Guinea pig, Pig, Rat
Clone
CBYC-A977
Antibody Isotype
IgG1
Application
IHC-Fr, IHC-P

Basic Information

Immunogen
Amylin
Specificity
Human, Cat, Guinea pig, Pig, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized from 100 mM PBS, 1% BSA, 0.1% sodium azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Islet Amyloid Polypeptide
Introduction
IAPP is a member of the calcitonin family of peptide hormones. This hormone is released from pancreatic beta cells following food intake to regulate blood glucose levels and act as a satiation signal. Human patients with type 1 and advanced type 2 diabete
Entrez Gene ID
Human3375
Cat751513
Rat24476
Guinea pig100135550
Pig100520838
UniProt ID
HumanP10997
CatP12967
RatP12969
Guinea pigP12966
PigD3Y4D2
Alternative Names
Islet Amyloid Polypeptide
Function
Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Biological Process
Adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: ARUK-UCL
Amylin receptor signaling pathway Source: ARUK-UCL
Amyloid fibril formation Source: UniProtKB
Apoptotic process Source: ProtInc
Cell-cell signaling Source: ProtInc
Eating behavior Source: Ensembl
Negative regulation of amyloid fibril formation Source: ARUK-UCL
Negative regulation of bone resorption Source: Ensembl
Negative regulation of cell differentiation Source: Ensembl
Negative regulation of cell population proliferation Source: UniProtKB
Negative regulation of mitochondrion organization Source: ARUK-UCL
Negative regulation of protein-containing complex assembly Source: ARUK-UCL
Positive regulation of apoptotic process Source: ARUK-UCL
Positive regulation of calcium ion import across plasma membrane Source: ARUK-UCL
Positive regulation of cell death Source: ARUK-UCL
Positive regulation of cytosolic calcium ion concentration Source: ARUK-UCL
Positive regulation of ERK1 and ERK2 cascade Source: ARUK-UCL
Positive regulation of gene expression Source: ARUK-UCL
Positive regulation of MAPK cascade Source: ARUK-UCL
Positive regulation of peptidyl-serine phosphorylation Source: ARUK-UCL
Positive regulation of protein kinase A signaling Source: ARUK-UCL
Positive regulation of protein kinase B signaling Source: ARUK-UCL
Protein destabilization Source: UniProtKB
Protein homooligomerization Source: UniProtKB
Sensory perception of pain Source: Ensembl
Signal transduction Source: ProtInc
Cellular Location
Secreted
PTM
Amyloid fibrils are degraded by IDE.

Xu, J., Jin, L., Chen, J., Zhang, R., Zhang, H., Li, Y., ... & Hu, C. (2022). Common variants in genes involved in islet amyloid polypeptide (IAPP) processing and the degradation pathway are associated with T2DM risk: A Chinese population study. Diabetes Research and Clinical Practice, 185, 109235.

Ferreira, S., Raimundo, A. F., Menezes, R., & Martins, I. C. (2021). Islet amyloid polypeptide & amyloid beta peptide roles in Alzheimer’s disease: two triggers, one disease. Neural regeneration research, 16(6), 1127.

Wang, Y., & Westermark, G. T. (2021). The amyloid forming peptides islet amyloid polypeptide and amyloid β interact at the molecular level. International Journal of Molecular Sciences, 22(20), 11153.

Raimundo, A. F., Ferreira, S., Martins, I. C., & Menezes, R. (2020). Islet amyloid polypeptide: a partner in crime with Aβ in the pathology of alzheimer's disease. Frontiers in Molecular Neuroscience, 13, 35.

Röder, C., Kupreichyk, T., Gremer, L., Schäfer, L. U., Pothula, K. R., Ravelli, R. B., ... & Schröder, G. F. (2020). Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils. Nature structural & molecular biology, 27(7), 660-667.

Armiento, V., Hille, K., Naltsas, D., Lin, J. S., Barron, A. E., & Kapurniotu, A. (2020). The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP). Angewandte Chemie International Edition, 59(31), 12837-12841.

Aftabizadeh, M., Tatarek-Nossol, M., Andreetto, E., El Bounkari, O., Kipp, M., Beyer, C., ... & Kapurniotu, A. (2019). Blocking inflammasome activation caused by β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP) through an IAPP mimic. ACS Chemical Neuroscience, 10(8), 3703-3717.

Hsu, Y. H., Chen, Y. W., Wu, M. H., & Tu, L. H. (2019). Protein glycation by glyoxal promotes amyloid formation by islet amyloid polypeptide. Biophysical Journal, 116(12), 2304-2313.

Oskarsson, M. E., Hermansson, E., Wang, Y., Welsh, N., Presto, J., Johansson, J., & Westermark, G. T. (2018). BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells. Proceedings of the National Academy of Sciences, 115(12), E2752-E2761.

Moore, S. J., Sonar, K., Bharadwaj, P., Deplazes, E., & Mancera, R. L. (2018). Characterisation of the structure and oligomerisation of islet amyloid polypeptides (IAPP): a review of molecular dynamics simulation studies. Molecules, 23(9), 2142.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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