Prion Protein (PrP) Fragments
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Prion Protein (PrP) Fragments

Browse products name by alphabetical order:

Cat. # Product Name Price
P10011 Scrambled PrP (106-126) Inquiry
P10010 PrP (89-106) Inquiry
P10009 PrP (57-64) Inquiry
P10008 PrP (200-223), Protease-Resistant Prion Protein (200-223), hamster Inquiry
P10007 PrP (166-179), Protease-Resistant Prion Protein (166-179), hamster Inquiry
P10005 PrP (127-147) Inquiry
P10004 PrP (117-136), Protease-Resistant Prion Protein (117-136), hamster Inquiry
P10003 PrP (113-126) Inquiry
P10002 PrP (106-126) Inquiry
P10001 PrP (106-114) Inquiry
P10013 Prion Protein (118-135) (human) Inquiry
P10012 Prion Protein (106-126) (human) (scrambled) Inquiry


Prion Protein (PrP) Fragments acts as a cell membrane surface glycoprotein consisting of approximately 250 amino acids, including the N-terminal signal peptide, five octapeptide repeats, a highly conserved hydrophobic region in the center of the protein, and a hydrophobic region at the C-terminus. PrP is involved in the transmembrane conduction, cell adhesion, copper ion metabolism, anti-apoptosis, anti-oxidative stress and other processes in vivo, and is also associated with the development of human and animal tumors, bacteria and viral diseases. Prion protein (PrP) exists in two different conformations: host-encoded, normal physiological cell prion protein (PrPC) and isomers of pathogenic prion protein: scrapie isoform of prion protein (commonly known as PrPSc). PrPc is a membrane protein expressed by normal cells and is highly conserved in mammals, mainly expressed in the nervous system and immune system. PrPSc plays a key role in the pathogenesis of prion diseases.

Mechanism of action

PrPc is involved in cell signaling in a high level of neurons and astrocytes present in the central nervous system (CNS) and plays an important role in regulating the nervous and immune systems. In addition, PrPc can mediate cell adhesion and signal transduction of Ca2+ independent progenitor antigens, and PrPc can regulate Ca2+ dependent cell adhesion by regulating the transport of E-cadherin to the plasma membrane. This is believed to have the property of adhesion molecules and is involved in a series of important physiological and pathological processes such as cell adhesion, membrane signal transduction, and cell stretching and movement. Therefore, abnormal expression or loss of function of PrPc has an important influence on tumor metastasis. For PrPSc, because it cannot be degraded by proteases, it gradually aggregates, causing degeneration of the central nervous system and eventually leading to death.

Application of Prion Protein (PrP) Fragments

PrP is overexpressed in cancers such as gastric cancer, pancreatic cancer, colorectal cancer, and breast cancer, affecting the occurrence, development, and invasion of these cancers, and is involved in many cellular processes. PrPc is involved in the development of human tumors and may become a new therapeutic target for various tumors. In the immune system, the endocrine system also plays an important role, and through the various physiological mechanisms and signaling pathways of PrPc, it can also provide new targets for the treatment of various diseases.

1. Málaga-Trillo, E., Solis, G. P., Schrock, Y., Geiss, C., Luncz, L., Thomanetz, V., & Stuermer, C. A. (2009). Regulation of embryonic cell adhesion by the prion protein. PLoS biology, 7(3), e1000055.
2. Peralta, O. A., & Eyestone, W. H. (2009). Quantitative and qualitative analysis of cellular prion protein (PrPC) expression in bovine somatic tissues. Prion, 3(3), 161-170.
3. Alleaume-Butaux, A., Dakowski, C., Pietri, M., Mouillet-Richard, S., Launay, J. M., Kellermann, O., & Schneider, B. (2013). Cellular prion protein is required for neuritogenesis: fine-tuning of multiple singaling pathways involved in focal adhesions and actin cytoskeleton dynamics. Cell Health and Cytoskeleton, 5, 1-12.

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