

| Catalog No. | HD759012 |
|---|---|
| Description |
Recombinant Human USP38 Protein, N-His (HD759012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Expression system | E. coli |
| Accession | Q8NB14 |
| Protein length | Met1-Ser420 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 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. |
| Alternate Names | Deubiquitinating enzyme 38, EC:3.4.19.12, HP43.8KD, KIAA1891, USP38, Ubiquitin carboxyl-terminal hydrolase 38, Ubiquitin thioesterase 38, Ubiquitin-specific-processing protease 38 |
| Background | Ubiquitin carboxyl-terminal hydrolase 38 is a ~116 kDa protein. Deubiquitinating enzyme that plays a role in various cellular processes, including DNA repair, cell cycle regulation, and immune response. Plays a role in the inhibition of type I interferon signaling by mediating the 'Lys-33' to 'Lys-48' ubiquitination transition of TBK1 leading to its degradation. Cleaves the ubiquitin chain from the histone demethylase LSD1/KDM1A and prevents it from degradation by the 26S proteasome, thus maintaining LSD1 protein level in cells. Plays a role in the DNA damage response by regulating the deacetylase activity of HDAC1. Mechanistically, removes the 'Lys-63'-linked ubiquitin chain promoting the deacetylase activity of HDAC1 in response to DNA damage. 1. Iphöfer, A. et al. (2012) Chembiochem : a European journal of chemical biology 13, 1416-20. PMID: 22689415 2. Liu, W. et al. (2018) Biological research 51, 53. PMID: 30497519 3. Yang, Y. et al. (2020) Cancer research 80, 719-731. PMID: 31874856 4. Yi, XM. et al. (2022) Proceedings of the National Academy of Sciences of the United States of America 119, e2116279119. PMID: 35238669 5. Lin, M. et al. (2016) Molecular cell 64, 267-281. PMID: 27692986 6. Zhan, W. et al. (2020) Oncogenesis 9, 48. PMID: 32404892 7. Xu, Z. et al. (2021) The international journal of biochemistry & cell biology 137, 106023. PMID: 34102342 |
| Note | For research use only |
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