Immunofluorescent analysis of ATP Synthase beta (green) in 3T3 cells. The cells were fixed with 4% paraformaldehyde for 15 minutes and blocked with 3% Blocker BSA (Product # 37525) in PBS for 15 minutes at room temperature. Cells were stained with or without ATP Synthase beta mouse monoclonal antibody (Product # MA1-930), at a concentration of 5ug/ml for 1 hour at room temperature, and then incubated with a Goat anti-Mouse IgG (H+L) Superclonal Secondary Antibody, Alexa Fluor® 488 conjugate (Product # A28175) at a dilution of 1:1000 for 1 hour at room temperature (both panels, green). Nuclei (both panels, blue) were stained with Hoechst 33342 dye (Product # 62249). Images were taken on a Thermo Scientific ToxInsight at 20X magnification.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rat, Mouse, Human|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Intact rat mitochondria.|
|Storage buffer||PBS with 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunofluorescence (IF)||1:100 - 1:1000|
|Immunoprecipitation (IP)||2-5 ug|
|Western Blot (WB)||1-2 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
MA1-930 detects the beta subunit of ATP synthase from mouse rat and human samples. This antibody is useful as a mitochondrial marker.
MA1-930 has been successfully used in immunofluorescence, western blot, and immunoprecipitation procedures. By immunoprecipitation, this antibody detects an 50 kDa protein representing ATP synthase from solubilized rat brain mitochondria.
ATP synthase is extremely conserved through evolution and can be found in plants, fungi, bacteria, and animals. The ATP synthase enzyme is a transmembrane protein responsible for driving the reversible reaction from ADP+ phosphate to ATP. This reaction is accomplished by a flux of protons across the membrane as a result of electron transfer.
The ATP synthase protein has two main sections; the F1 ATP-ase (soluble) and the F0 ATP-ase (membrane embedded). The F1 section consists of the alpha, beta, gamma, delta, and epsilon subunits. While the F0 consists of a, b, and c subunits.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis.
MA1-930 was used in immunohistochemistry to study the contribution of mitochondrial function to idiopathic pulmonary fibrosis pathogenesis.
|Bueno M,Lai YC,Romero Y,Brands J,St Croix CM,Kamga C,Corey C,Herazo-Maya JD,Sembrat J,Lee JS,Duncan SR,Rojas M,Shiva S,Chu CT,Mora AL||The Journal of clinical investigation (125:521)||2015|
Human brain endothelial ATP synthase beta-subunit is mannose-insensitive binding target of FimH.
MA1-930 was used in western blot to investigate the molecular mechanism for the binding of E.coli to human brain microvascular endothelial cells
|Shin S,Kim KS||FEMS microbiology letters (303:156)||2010|
The Krebs cycle and mitochondrial mass are early victims of endothelial dysfunction: proteomic approach.
MA1-930 was used in western blot to study the progression of endothelial cell dysfunction.
|Addabbo F,Ratliff B,Park HC,Kuo MC,Ungvari Z,Csiszar A,Ciszar A,Krasnikov B,Krasnikof B,Sodhi K,Zhang F,Nasjletti A,Goligorsky MS||The American journal of pathology (174:34)||2009|
Polyamine transport by mammalian cells and mitochondria: role of antizyme and glycosaminoglycans.
MA1-930 was used in western blot to investigate the roles of antizyme and glycosaminoglycans during the polyamine transport in mammalian cells and mitochondria.
|Hoshino K,Momiyama E,Yoshida K,Nishimura K,Sakai S,Toida T,Kashiwagi K,Igarashi K||The Journal of biological chemistry (280:42801)||2005|
Expression and subcellular localization of BNIP3 in hypoxic hepatocytes and liver stress.
MA1-930 was used in immunocytochemistry to study the association between the upregulation of BNIP3 and the hepatocyte cell death
|Metukuri MR,Beer-Stolz D,Namas RA,Dhupar R,Torres A,Loughran PA,Jefferson BS,Tsung A,Billiar TR,Vodovotz Y,Zamora R||American journal of physiology. Gastrointestinal and liver physiology (296:G499)||2009|