LMP2/PSMB9 Antibody (OTI1D1) [mFluor Violet 450 SE]

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. Other proteins are degraded via the vacuolar pathway which includes endosomes, lysosomes, and the endoplasmic reticulum. The 26S proteasome is an ATP-dependent, multisubunit (~31), barrel-shaped molecular machine with an apparent molecular weight of ~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. The PA28/11S REG Activator protein complex functions as a proteolytic activator. LMP2 is a catalytic subunit of the 20S proteasome and, upon interferon gamma-induction, replaces the delta subunit. LMP2 alters the specificity of the 20S proteasome and is critical for the production of MHC class I ligands, production of T-lymphocytes, and is suggested to increase the efficiency of antigen presentation of the immune response. Several genetic diseases are associated with defects in the ubiquitin-proteasome pathway. Some examples of affected proteins include those linked to cystic fibrosis (CF transmembrane regulator), Angelman's syndrome (E6-AP), and Liddle syndrome (endothelial sodium channels).

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Array NBP2-71261MFV450

• LMP2/PSMB9 Antibodies
• LMP2/PSMB9 Lysate
• LMP2/PSMB9 Proteins