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Sino Biological Inc. liefert USP30 Protein (N-SUMO Tag) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.
Weitere Informationen über USP30 Protein (N-SUMO Tag) lesen Sie bitte: http://www.sinobiological.com/USP30-Protein-g-10548.html
| Synonym | USP30 |
| Protein Construction | A DNA sequence encoding the human USP30 (Thr48 - Glu508) was fused with the SUMO tag at the N-terminus. |
| Source | Human |
| Expression Host | Baculovirus-Insect cells |
| Purity | > 95 % as determined by SDS-PAGE | SDS-PAGE:![]() USP30 protein |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method | |
| Stability | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal | Met | |
| Molecular Mass | The secreted recombinant human USP30 consists of 580 amino acids and predicts a molecular mass of 66.3 KDa. The apparent molecular mass of the protein is approximately 87 KDa in SDS-PAGE under reducing conditions due to glycosylation. | |
| Formulation | Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% gly.
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| Storage | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
Ubiquitin specific peptidase 30, also known as USP30, is a deubiquitinating enzyme that is embedded in the mitochondrial outer membrane. USP30 participates in the maintenance of mitochondrial morphology, a finding that provides new insight into the cellular function of deubiquitination. Depletion of USP30 expression by RNA interference induced elongated and interconnected mitochondria, depending on the activities of the mitochondrial fusion factors mitofusins, without changing the expression levels of the key regulators for mitochondrial dynamics. Mitochondria were rescued from this abnormal phenotype by ectopic expression of USP30 in a manner dependent on its enzymatic activity.