ATP5G1 Antibody
Rabbit mAb
- 产品详情
- 实验流程
Application
| WB, IF, ICC |
|---|---|
| Primary Accession | P05496 |
| Reactivity | Rat, Human, Mouse |
| Clonality | Monoclonal |
| Other Names | ATP5A; ATP5G1; ATPase protein 9; ATPase subunit 9; ATPase subunit c; |
| Isotype | Rabbit IgG |
| Host | Rabbit |
| Calculated MW | 14277 Da |
| Dilution | WB 1:500~1:2000 ICC/IF 1:50~1:200 |
|---|---|
| Purification | Affinity-chromatography |
| Immunogen | A synthesized peptide derived from human ATP5G1 |
| Description | Mitochondrial membrane ATP synthase (F1F0 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. |
| Storage Condition and Buffer | Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | ATP5MC1 (HGNC:841) |
|---|---|
| Function | Subunit c, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). With the subunit a (MT- ATP6), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix (PubMed:37244256). Protons are taken up via the inlet half- channel and released through the outlet half-channel, following a Grotthuss mechanism (PubMed:37244256). |
| Cellular Location | Mitochondrion membrane; Multi-pass membrane protein |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
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