ITA4687
ITA4687
- Catalog: ITA4687
- Gene/Protein: ATP5L2
- Product Description: Immunotag™ ATP5L2 Antibody
385.0000
Price in reward points: 385
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Antibody Specification | |
Datasheet | |
Target Protein | ATP5L2 |
Clonality | Polyclonal |
Storage/Stability | -20°C/1 year |
Application | WB,IF/ICC,ELISA |
Recommended Dilution | WB 1:500~1:1000 IF/ICC 1:100-1:500 |
Concentration | 1 mg/ml |
Reactive Species | Human |
Host Species | Rabbit |
Immunogen | A synthesized peptide |
Specificity | ATP5L2 Antibody detects endogenous levels of total ATP5L2 |
Purification | The antiserum was purified by peptide affinity chromatography. |
Form | Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt |
Gene Name | ATP5L2 |
Accession No. | Q7Z4Y8 |
Alternate Names | AT5L2_HUMAN; ATP synthase H+ transporting mitochondrial F0 complex subunit G2 pseudogene; ATP synthase H+ transporting mitochondrial F1F0 subunit g; ATP synthase H+ transporting mitochondrial Fo complex subunit G2; ATP synthase subunit g 2; ATP synthase subunit g 2 mitochondrial; ATP5K2; ATP5L2; ATPase subunit g 2; mitochondrial; |
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. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane (By similarity). |
Cell Pathway/ Category | Primary Polyclonal Antibody |
Protein MW | 20 KD |
Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |