Anti-UchL1, clone SPM575

1 mg/ml in sterile PBS, BSA free, sodium azide free. This mAb reacts with a protein of 20-30kDa, identified as PGP9.5, also known as ubiquitin carboxyl-terminal hydrolase-1 (UchL1). Initially, UchL1 expression in normal tissues was reported in neurons and neuroendocrine cells but later it was found in distal renal tubular epithelium, spermatogonia, Leydig cells, oocytes, melanocytes, prostatic secretory epithelium, ejaculatory duct cells, epididymis, mammary epithelial cells, Merkel cells, and dermal fibroblasts. Furthermore, immunostaining for UchL1 has been shown in a wide variety of mesenchymal neoplasms as well. A mutation in the gene is believed to cause a form of Parkinson's disease. Protein function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. [The UniProt Consortium]