Recombinant Human ATPB protein (Tagged) is a Human Fragment protein, in the 230 to 529 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Publications
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- Cell 183:76-93.e222020Targeting Mitochondria-Located circRNA SCAR Alleviates NASH via Reducing mROS Output.Applications:Unspecified applicationReactive species:Unspecified reactive speciesQiyi Zhao,Jiayu Liu,Hong Deng,Ruiying Ma,Jian-You Liao,Huixin Liang,Jingxiong Hu,Jiaqian Li,Zhiyong Guo,Junchao Cai,Xiaoding Xu,Zhiliang Gao,Shicheng SuPubMed 32931733
Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
Y S V F A G V G E R T R E G N D L Y H E M I E S G V I N L K D A T S K V A L V Y G Q M N E P P G A R A R V A L T G L T V A E Y F R D Q E G Q D V L L F I D N I F R F T Q A G S E V S A L L G R I P S A V G Y Q P T L A T D M G T M Q E R I T T T K K G S I T S V Q A I Y V P A D D L T D P A P A T T F A H L D A T T V L S R A I A E L G I Y P A V D P L D S T S R I M D P N I V G S E H Y D V A R G V Q K I L Q D Y K S L Q D I I A I L G M D E L S E E D K L T V S R A R K I Q R F L S Q P F Q V A E V F T G H M G K L V P L K E T I K G F Q Q I L A G E Y D H L P E Q A F Y M V G P I E E A V A K A D K L A E E H S S
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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 synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). 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.
Alternative names
ATP5B, ATPMB, ATPSB, ATP5F1B, ATP synthase F1 subunit beta
Recommended products
Recombinant Human ATPB protein (Tagged) is a Human Fragment protein, in the 230 to 529 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- P06576-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Sequence info
Amino acid sequence
- Y S V F A G V G E R T R E G N D L Y H E M I E S G V I N L K D A T S K V A L V Y G Q M N E P P G A R A R V A L T G L T V A E Y F R D Q E G Q D V L L F I D N I F R F T Q A G S E V S A L L G R I P S A V G Y Q P T L A T D M G T M Q E R I T T T K K G S I T S V Q A I Y V P A D D L T D P A P A T T F A H L D A T T V L S R A I A E L G I Y P A V D P L D S T S R I M D P N I V G S E H Y D V A R G V Q K I L Q D Y K S L Q D I I A I L G M D E L S E E D K L T V S R A R K I Q R F L S Q P F Q V A E V F T G H M G K L V P L K E T I K G F Q Q I L A G E Y D H L P E Q A F Y M V G P I E E A V A K A D K L A E E H S S
- Accession
- P06576
- Protein length
- Fragment
- Predicted molecular weight
- 52.8 kDa
- Amino acids
- 230 to 529
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
General info
- 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 synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). 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.
- Sequence similarities
Belongs to the ATPase alpha/beta chains family.
- Subcellular localisation
- Mitochondrion inner membrane
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage conditions
- -20°C
- Appropriate long-term storage conditions
- -20°C
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
ATPB also known as ATP synthase subunit beta is an essential protein component of the ATP synthase complex. It has an approximate mass of 52 kDa and is primarily expressed in the mitochondria. The protein's role is to catalyze the production of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate utilizing the proton gradient across the inner mitochondrial membrane. This process is central to the cellular energy production often referred to as oxidative phosphorylation. ATPB is frequently used as a mitochondrial marker in research making it an important target for antibodies such as those conjugated with Alexa Fluor 647 for immunofluorescence applications.
- Biological function summary
ATPB functions as part of the mitochondrial ATP synthase complex which is also known as complex V of the electron transport chain. This complex is important for maintaining cellular energy homeostasis through ATP production. ATPB contributes to the catalytic activity necessary for ATP synthesis therefore supporting various cellular processes that require energy input such as muscle contraction and active transport. The protein also plays a role in coupling the proton motive force to ATP synthesis a function critical for mitochondrial efficiency and metabolic health.
- Pathways
ATPB involves itself significantly in the oxidative phosphorylation and glycolysis pathways. It partners with other proteins in the ATP synthase complex such as ATP synthase subunit alpha (ATP5A1) to effectuate the conversion of energy. In the broader scope of energy metabolism ATPB integrates with glycolysis where glycolytic end-products feed into oxidative phosphorylation sustaining the cell’s energy currency. Both pathways are important for cells especially in tissues with high energy demands like the heart and skeletal muscles.
- Associated diseases and disorders
ATPB has been implicated in mitochondrial dysfunction-related diseases such as mitochondrial myopathy and Leigh syndrome. These conditions often result from mutations or defects in components of the electron transport chain leading to impaired ATP production. ATPB’s close connection to ATP5A1 and other complex V proteins highlights its involvement in these disorders. Understanding ATPB's role and function helps in disease mechanism elucidation and potentially offers targets for therapeutic interventions in mitochondrial-related diseases.
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1 product image
SDS-PAGE - Recombinant Human ATPB protein (Tagged) (ab235856)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel of ab235856.
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