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Results for "

β-sheet protein

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Amylin Receptor (1) Lipocalin Family (1) Prion Protein (1)
By Research Areas:	Infection (1) Inflammation/Immunology (1) Neurological Disease (2)

Inhibitors & Agonists

Biochemical Assay Reagents

Peptides

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-NP008

β-Lactoglobulin	Lipocalin Family	Inflammation/Immunology
β-Lactoglobulin, a major whey protein, is a small globular protein from the lipocalin family. β-Lactoglobulin is an important source of the essential and branched-chain amino acids (leucine, isoleucine, and valine). β-Lactoglobulin shows antioxidant properties, because it contains two disulfide bonds and one free thiol group. β-Lactoglobulin is a ligand transport agent. β-Lactoglobulin is one of the major allergens in milk and can be utilized in the research for developing safe hypoallergenic dairy products .

HY-P10534

ccβ	Prion Protein	Infection Neurological Disease
CCβ is a simple 17-amino acid peptide designed in research. CCβ is able to mimic the conformational transition of proteins from α-helix to β-sheet, which is a key step in the aggregation of proteins associated with many diseases, such as Alzheimer's disease and prion disease. CCβ can be used to study diseases related to protein aggregation .

HY-P4873

Amylin (20-29) (human)	Amylin Receptor	Neurological Disease
Amylin (20-29) (human) is the fragment of human islet amyloid polypeptide (hIAPP) or Amylin. Amylin is a 37-residue hormone. Amylin (20-29) (human) is responsible for the amyloidogenic propensities of the full length protein. Amylin (20-29) (human) can be transformed into its corresponding peptoid and retropeptoid sequences, to obtain beta-sheet breaker peptides as amyloid inhibitors .

Cat. No.	Product Name	Type

HY-NP008

β-Lactoglobulin	Native Proteins
β-Lactoglobulin, a major whey protein, is a small globular protein from the lipocalin family. β-Lactoglobulin is an important source of the essential and branched-chain amino acids (leucine, isoleucine, and valine). β-Lactoglobulin shows antioxidant properties, because it contains two disulfide bonds and one free thiol group. β-Lactoglobulin is a ligand transport agent. β-Lactoglobulin is one of the major allergens in milk and can be utilized in the research for developing safe hypoallergenic dairy products .

β-Lactoglobulin

Native Proteins

β-Lactoglobulin, a major whey protein, is a small globular protein from the lipocalin family. β-Lactoglobulin is an important source of the essential and branched-chain amino acids (leucine, isoleucine, and valine). β-Lactoglobulin shows antioxidant properties, because it contains two disulfide bonds and one free thiol group. β-Lactoglobulin is a ligand transport agent. β-Lactoglobulin is one of the major allergens in milk and can be utilized in the research for developing safe hypoallergenic dairy products .

Cat. No.	Product Name	Target	Research Area

HY-P10534

ccβ	Prion Protein	Infection Neurological Disease
CCβ is a simple 17-amino acid peptide designed in research. CCβ is able to mimic the conformational transition of proteins from α-helix to β-sheet, which is a key step in the aggregation of proteins associated with many diseases, such as Alzheimer's disease and prion disease. CCβ can be used to study diseases related to protein aggregation .

HY-P4873

Amylin (20-29) (human)	Amylin Receptor	Neurological Disease
Amylin (20-29) (human) is the fragment of human islet amyloid polypeptide (hIAPP) or Amylin. Amylin is a 37-residue hormone. Amylin (20-29) (human) is responsible for the amyloidogenic propensities of the full length protein. Amylin (20-29) (human) can be transformed into its corresponding peptoid and retropeptoid sequences, to obtain beta-sheet breaker peptides as amyloid inhibitors .

HY-P5340

Amyloid-Forming peptide GNNQQNY	Peptides	Others
Amyloid-Forming peptide GNNQQNY is a biological active peptide. (This is a heptapeptide from the N-terminal prion-determining domain of the yeast protein Sup35 that forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. The GNNQQNY dimer forms three stable sheet structures. in-register parallel, off-register parallel, and anti-parallel. The in-register parallel dimer, which is close to the amyloid beta-sheet structure, has few interpeptide hydrogen bonds, making hydrophobic interactions more important and increasing the conformational entropy compared to the anti-parallel sheet.)

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