Recombinant Human UfSP1 protein is a Human Full Length protein, in the 1 to 142 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Thiol-dependent isopeptidase that specifically mediate the processing of UFM1 precursors as well as the deconjugation of UFM1 from target proteins (PubMed:35525273, PubMed:35926457). Mainly responsible for the maturation of the UFM1 precursor, a prerequisite for conjugation reactions (PubMed:35525273, PubMed:35926457).
Ufm1-specific protease 1, UfSP1, UFSP1
Recombinant Human UfSP1 protein is a Human Full Length protein, in the 1 to 142 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8.5
Constituents: 30% Glycerol (glycerin, glycerine), 1.17% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab139220 is purified using conventional chromatography techniques.
Thiol-dependent isopeptidase that specifically mediate the processing of UFM1 precursors as well as the deconjugation of UFM1 from target proteins (PubMed:35525273, PubMed:35926457). Mainly responsible for the maturation of the UFM1 precursor, a prerequisite for conjugation reactions (PubMed:35525273, PubMed:35926457).
Belongs to the peptidase C78 family.
UfSP1 also known as UfSP domain-containing protein 1 is an enzyme that functions mechanically as a cysteine protease. It specifically catalyzes the cleavage of the ubiquitin-fold modifier 1 (UFM1) from its substrates during post-translational modifications. UfSP1 has a molecular mass of about 50 kDa and is expressed in various tissues but shows significant presence in the liver and kidney. Its activity is essential for the processing and function of proteins modified by UFM1 conjugation.
UfSP1 plays an important role in cellular processes such as UFMylation an ubiquitin-like modification system. It acts as part of a larger protein complex responsible for maintaining protein homeostasis. UfSP1's function ensures that proteins tagged with UFM1 undergo precise activation and deactivation which is critical for the cellular machinery's smooth operations. By removing UFM1 UfSP1 also helps regulate protein folding degradation and endoplasmic reticulum (ER) stress responses.
UfSP1 takes part in the endoplasmic reticulum (ER) stress response and UFM1 modification pathway. This enzyme directly interacts with UFM1-specific E1 and E2 enzymes linking it to protein homeostasis and stress management pathways. Through its activity UfSP1 influences protein quality control which is associated with the ER-associated degradation (ERAD) pathway. UfSP1 ensures the proper recycling of UFM1 avoiding unnecessary stress responses and degradation.
UfSP1 has been implicated in conditions such as neurodegenerative diseases and cancer. It plays a role in cellular stress management and dysregulation of UfSP1 activity can lead to accumulation of misfolded proteins contributing to neurodegenerative disorders like Alzheimer's disease. Moreover abnormal UFM1 pathway activities where UfSP1 is an important player have been observed in cancer pathogenesis with proteins like UFM1 and its conjugating enzymes engaged in tumor growth and survival. Understanding UfSP1's role offers insights into potential therapeutic strategies for these conditions.
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15% SDS-PAGE analysis of ab139220 (3μg).
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