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AB224139

Anti-ATP5J antibody

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(3 Publications)

Rabbit Polyclonal ATP5J antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human ATP5PF aa 1-150.

View Alternative Names

ATP5A, ATP5J, ATPM, ATP5PF, ATPase subunit F6, ATP synthase peripheral stalk subunit F6

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-ATP5J antibody (AB224139)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-ATP5J antibody (AB224139)

PFA-fixed, Triton X-100 permeabilized U-2 OS (human bone osteosarcoma epithelial cell line) cells stained for ATP5J (green) using ab224139 at 4 μg/ml in ICC/IF.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ATP5J antibody (AB224139)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ATP5J antibody (AB224139)

Paraffin-embedded human liver tissue stained for ATP5J using ab224139 at 1/500 dilution in immunohistochemical analysis.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ICC/IF, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human ATP5PF aa 1-150. The exact immunogen used to generate this antibody is proprietary information.

P18859

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ATP5J also known as ATP synthase subunit F6 is a part of the mitochondrial ATP synthase complex. The ATP5J protein has a mass of about 11 kDa. It is expressed mainly in the inner mitochondrial membrane where it plays an integral role in the process of synthesizing ATP from ADP and inorganic phosphate. ATP5J interacts directly with other subunits of the ATP synthase complex contributing to the functional structure of this vital enzyme complex.
Biological function summary

ATP5J functions in tandem with other components of the ATP synthase complex to facilitate energy production in cells. This complex also known as Complex V catalyzes the final step in oxidative phosphorylation a critical process for cellular energy generation. ATP5J ensures the proper assembly and structural integrity of the ATP synthase complex playing a role in the efficient conversion of the proton motive force into mechanical energy which drives the production of ATP.

Pathways

ATP5J is central to oxidative phosphorylation and ATP synthesis pathways. It interacts closely with key proteins like ATP5A and ATP5B within this pathway. These interactions enable the transduction of electrochemical gradients into usable cellular energy. Furthermore ATP5J's role ensures that ATP synthase maintains its efficiency in energy conversion which is important for meeting cellular metabolic demands.

Mutations or malfunctions of ATP5J can contribute to mitochondrial diseases such as mitochondrial encephalomyopathy. Dysregulation of ATP5J might also relate to disorders like Leigh syndrome where defects in oxidative phosphorylation are common. Other proteins such as COX5A and NDUFS6 also play roles in these conditions highlighting the interconnected nature of mitochondrial function and its impact on human health.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Subunit F6, 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 (PubMed : 37244256). 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). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed : 37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
See full target information ATP5PF

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Experimental and therapeutic medicine 22:1185 PubMed34475975

2021

Detection of mitochondrial coupling factor 6 in placental tissues from preeclamptic pregnancies and its influence on biological behavior of trophoblast cells.

Applications

Unspecified application

Species

Unspecified reactive species

Wanyu Song,Xufeng Shi,Kan Liu,Ranhong Li,Leilei Niu,Lijun Su,Haiying Wu

Proceedings of the National Academy of Sciences of the United States of America 118: PubMed33431668

2021

ATRX and RECQ5 define distinct homologous recombination subpathways.

Applications

Unspecified application

Species

Unspecified reactive species

Amira Elbakry,Szilvia Juhász,Ki Choi Chan,Markus Löbrich

Cancer research 80:524-535 PubMed31690671

2019

Acquired Resistance to HER2-Targeted Therapies Creates Vulnerability to ATP Synthase Inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

Molly Gale,Yao Li,Jian Cao,Zongzhi Z Liu,Marissa A Holmbeck,Meiling Zhang,Sabine M Lang,Lizhen Wu,Mariana Do Carmo,Swati Gupta,Keisuke Aoshima,Michael P DiGiovanna,David F Stern,David L Rimm,Gerald S Shadel,Xiang Chen,Qin Yan
View all publications

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