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PEP-158 is a 14 amino acid synthetic peptide whose sequence is from human proteasome 11S REG beta. The sequence of this peptide is (amino to carboxy terminus): M (1)-A-K-P-C-G-V-R-L-S-G-E-A-R (14)
This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and human proteasome 11S REG beta, catalog # PA1-976. Using a solution with equal weights per unit volume of peptide and corresponding antibody will yield a solution with a large molar excess of peptide that is able to competitively bind the antibody.
Reconstitute with 0.1 mL of distilled water.
Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes, and the endoplasmic reticulum. The 26S proteasome is an ATP-dependent, multisubunit (approximately 31), barrel-shaped molecular machine with an apparent molecular weight of approximately 2.5 MDa. It consists of a 20S proteolytic core complex which is crowned at one or both ends by 19S regulatory subunit complexes. The 19S regulatory subunits recognize ubiquitinated proteins and play an essential role in unfolding and translocating targets into the lumen of the 20S subunit. An enzymatic cascade is responsible for the attachment of multiple ubiquitin molecules to lysine residues of proteins targeted for degradation. Several genetic diseases are associated with defects in the ubiquitin-proteasome pathway. Some examples of affected proteins include those linked to cystic fibrosis, Angelman's syndrome, and Liddle syndrome.
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