Recombinant Protein of Human MRPL22, aa 41-206(Cat#: RIJL-0225-JL413)
This product is a recombinant human MRPL22 protein with specific tag. It is availible for SDS-PAGE, WB, immunogen, bioactivity testing and ELISA.
Certificate of Analysis (COA)
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Lot Number
Summary
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Description
| This product is a recombinant human MRPL22 protein with specific tag. It is availible for SDS-PAGE, WB, immunogen, bioactivity testing and ELISA. |
Product Property
| Species Reactivity | Human |
| Molecule Mass | 14.5 kDa |
| Purity | >85% determined by SDS-PAGE |
| Endotoxin | <1.0EU per 1µg (determined by the LAL method) |
| Expression Host | E.coli |
| Formulation | Tris/PBS-based buffer, 6% Trehalose |
| Residues | 41-206aa |
| Sequence | ISRKWEKKNKIVYPPQLPGEPRRPAEIYHCRRQIKYSKDKMWYLAKLIRGMSIDQALAQLEFNDKKGAKIIKEVLLEAQDMAVRDHNVEFRSNLYIAESTSGRGQCLKRIRYHGRGRFGIMEKVYCHYFVKLVEGPPPPPEPPKTAVAHAKEYIQQLRSRTIVHTL |
| Product Form | Lyophilized powder |
| Tags | Tag type will be determined during the manufacturing process. |
| Type | Recombinant Protein |
| Applications | SDS-PAGE; WB; Immunogen; Bioactivity Testing; ELISA |
| Storage | Store at -20°C/-80°C. Avoid freeze-thaw cycles. |
Target
| Alternative Names | Mitochondrial Ribosomal Protein L22; RPML25; Large Ribosomal Subunit Protein UL22m; Mitochondrial Large Ribosomal Subunit Protein UL22m; MRPL25 |
| Gene ID | 29093 |
| UniProt ID | Q9NWU5 |
| Location | Mitochondrion |
| Introduction | MRPL22, or Mitochondrial Ribosomal Protein L22, serves as a vital component within the large ribosomal subunit of the mitochondrial ribosome in eukaryotic cells. It plays a crucial role in facilitating the translation of mitochondrial genes, which is indispensable for the production of proteins involved in energy generation through oxidative phosphorylation. Alterations or deficiencies in MRPL22 can disrupt the mitochondrial translational process, potentially impacting cellular energy production and leading to mitochondrial disorders. |
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For Research Use Only. Not for Diagnostic or Therapeutic Applications.
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