Ubiquitin Carboxyl-Terminal Hydrolase 14/USP14 Protein(N-6His) (recombinant human)

Protein Construction: Recombinant Human Ubiquitin Carboxyl-Terminal Hydrolase 14 is produced by our E.coli expression system and the target gene encoding Asp91-Gln494 is expressed with a 6His tag at the N-terminus. Sequence: Asp91-Gln494. Fusion tag: N-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 52 kDa. Protein function: Ubiquitin Carboxyl-Terminal Hydrolase 14 (USP14) belongs to the ubiquitin-specific processing (USP) family which is a deubiquitinating enzyme (DUB) with His and Cys domains. USP14 located in the cytoplasm is a proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. USP14 acts also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. In addition, USP14 is indispensable for synaptic development and function at neuromuscular junctions, required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Protein function: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation. [The UniProt Consortium]