R&D Systems代理E-544-025 Recombinant Human USP14 Protein, CF (25 UG)

2025-06-28

货号:E-544-025

品牌:R&D Systems

规格:25ug

目录价:¥1570.00

市场价格:¥1256.00

会员价格:¥1256.00

  • 到货时间:3~4周

    金山科研平台,产品价格货期咨询微信:jinshanbio Source:E. coli-derived, Accession #:P54578 Purity:>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain. Predicted Molecular Mass:56 kDa Activity:Recombinant Human USP14 is a Ubiquitin-specific deconjugating enzyme. The activity of Recombinant Human USP14 was measured at 2.0 RFU/min/µg using an enzyme concentration of 18 µM and a Ub-AMC concentration of 4 µM in 100 mM HEPES, pH 8.5, 10 mM DTT, and 5% Glycerol at 25 °C. USP14 activity is greatly stimulated in the presence of 19S proteasome. Formulation:Supplied as a solution in HEPES, NaCl, DTT and EDTA.See Certificate of Analysis for details. Molecule Information: USP14 Long Name: Ubiquitin Specific Protease 14 Aliases: TGT; Ubiquitin Thioesterase 14; Ubp6 Entrez Gene IDs: 9097 (Human); 59025 (Mouse); 291796 (Rat) Background: USP14 Ubiquitin Specific Peptidase 14 (USP14) is a cytoplasmic protein that belongs to the peptidase C19 family of deubiquitinating enzymes. It has a predicted molecular weight of 56.1 kDa. Human USP14 is 494 amino acids (aa) in length, contains an N-terminal Ubiquitin-like (Ubl) domain (4-80 aa), and shares 97% aa sequence identity with the mouse and rat orthologs. USP14 is one of three deubiquitinating enzymes associated with the 26S Proteasome. It reversibly binds the 19S regulatory particle via its Ubl domain and mediates the disassembly of Ubiquitin chains on substrates by the stepwise removal of Ubiquitin molecules from the distal tip of the chain. USP14 has also been shown to deubiquitinate the chemokine receptor CXCR4, regulating both CXCL12/SDF-1-induced chemotaxis and receptor degradation. USP14 appears to be critical for the development and function of neuromuscular junctions. Additionally, USP14 is thought to serve as a physiological inhibitor of endoplasmic reticulum-associated degradation under non-stressed conditions by inhibiting the degradation of unfolded endoplasmic reticulum proteins.

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