

| Catalog No. | HX186014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human, Mouse | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Clonality | Polyclonal | ||||||||
| Isotype | IgG | ||||||||
| Immunogen | E. coli - derived recombinant Human USP14 (Met1-Gln494). | ||||||||
| Target | Deubiquitinating enzyme 14, TGT, Ubiquitin thioesterase 14, Ubiquitin carboxyl-terminal hydrolase 14, Ubiquitin-specific-processing protease 14, USP14 | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P54578 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Ubiquitin carboxyl-terminal hydrolase 14 (USP14) is a ~56 kDa protein. 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. Also serves 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. 1. Liu, D. et al. (2022) Proceedings of the National Academy of Sciences of the United States of America 119. PMID: 35145029 2. Koulich, E. et al. (2008) Molecular biology of the cell 19, 1072-82. PMID: 18162577 3. Kuo, CL. et al. (2017) Proceedings of the National Academy of Sciences of the United States of America 114, E3404-E3413. PMID: 28396413 4. Mines, MA. et al. (2009) The Journal of biological chemistry 284, 5742-52. PMID: 19106094 5. Nagai, A. et al. (2009) Biochemical and biophysical research communications 379, 995-1000. PMID: 19135427 6. Chen, M. et al. (2016) Molecular cell 64, 105-119. PMID: 27666593 | ||||||||
| Note | For research use only. |
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