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Results for "

N-terminal domain

" in MedChemExpress (MCE) Product Catalog:

24

Inhibitors & Agonists

1

Screening Libraries

5

Peptides

1

Inhibitory Antibodies

1

Natural
Products

4

Recombinant Proteins

3

Antibodies

Cat. No. Product Name Target Research Area
  • HY-P10152
    INF7

    		Peptides Infection
    INF7 is a derivative of the N-terminal domain of the HA2 protein that can be used to enhance the endosomal escape of polyplexes or liposome-encapsulated proteins .
  • HY-P2490
    Acetyl-Hirudin (54-65) (sulfated)

    		Peptides Metabolic Disease
    Acetyl-Hirudin (54-65) (sulfated) is a acetyl-fragment of Hirudin which binds directly to thrombin-rHCII(L444R) and disrupts interactions between the N-terminal acidic domain of rHCII and anion-binding exosite I of thrombin that serves to stabilize the complex .
  • HY-P5320
    TAT-BH4 (Bcl-xL)

    		Apoptosis Others
    TAT-BH4 (Bcl-xL) localized mainly at the mitochondria, prevents apoptotic cell death. TAT-BH4 (Bcl-xL) is a fusion peptide that combines the N-terminal cysteine conjugated protein transduction domain of HIV TAT protein (amino acids 49 to 57) with the Bcl-xL BH4 peptide. TAT-BH4 can be used for research of diseases caused by accelerated apoptosis .
  • HY-P5320A
    TAT-BH4 (Bcl-xL) (TFA)

    		Apoptosis Others
    TAT-BH4 (Bcl-xL) TFA is localized mainly at the mitochondria, prevents apoptotic cell death. TAT-BH4 (Bcl-xL) is a fusion peptide that combines the N-terminal cysteine conjugated protein transduction domain of HIV TAT protein (amino acids 49 to 57) with the Bcl-xL BH4 peptide. TAT-BH4 TFA can be used for research of diseases caused by accelerated apoptosis .
  • 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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