Recombinant Human Atp Synthase Subunit Delta, Mitochondrial (ATP5D) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-03352P

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5D.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5D.
Recombinant Human Atp Synthase Subunit Delta, Mitochondrial (ATP5D) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-03352P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Atp Synthase Subunit Delta, Mitochondrial (ATP5D) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P30049 |
Target Symbol | ATP5D |
Synonyms | ATP synthase subunit delta; mitochondrial ; ATP synthase subunit delta; mitochondrial; ATP synthase; H+ transporting; mitochondrial F1 complex; delta subunit; ATP5D; ATPD_HUMAN; F ATPase delta subunit ; F-ATPase delta subunit; Mitochondrial ATP synthase complex delta subunit precusor ; Mitochondrial ATP synthase delta subunit |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | AEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE |
Expression Range | 23-168aa |
Protein Length | Full Length of Mature Protein |
Mol. Weight | 31.0kDa |
Research Area | Metabolism |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. |
Subcellular Location | Mitochondrion. Mitochondrion inner membrane. |
Protein Families | ATPase epsilon chain family |
Database References |
Gene Functions References
- These data establish c.245C>T (p.Pro82Leu) and c.317T>G (p.Val106Gly) in ATP5F1D as pathogenic variants leading to a Mendelian mitochondrial disease featuring episodic metabolic decompensation. PMID: 29478781
- Immunohistochemical and immunofluorescent double staining of ATP5D and synaptophysin showed that the reduction of ATP5D was most pronounced at synapses in amyotrophic lateral sclerosis PMID: 27899032