Select country change
Shopping cart (0 , 0,00 ) Menu Search
Manufactured by BioVendor

ATPase Inhibitor Mitochondrial Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Inhibitor of F(1)F(o)-ATPase, IF(1), IF1
  • Species:Human
Please select your region to see available products and prices.
Cat. No. Size Price


RD191392200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Tissue extract, Plasma (EDTA, citrate, heparin)

Sample Requirements

35 µl/well

Storage/Expiration

Store the complete kit at 2 8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

6.25 – 400 pg/ml

Limit of Detection

1 pg/ml

Intra-assay (Within-Run)

n = 8; CV = 4.2 %

Inter-assay (Run-to-Run)

n = 6; CV = 9.1 %

Spiking Recovery

98.2 %

Dilutation Linearity

93.9 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3.5 hours
  • The kit measures IF1 in serum, plasma (EDTA, citrate, heparin) and tissue extract
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Oncology

Summary

IF1 (ATPase Inhibitor Mitochondrial, Inhibitor of F(1)F(0)-ATPase) is an endogenous inhibitor protein of mitochondrial ATP synthase. The ATP synthase (F1F0-ATPsynthase) is an important enzyme that catalyzes the synthesis of ATP (oxidative phosphorylation) utilizing the energy produced by the trans-membrane electrochemical proton gradient along the respiratory chain. ATP synthase is comprised of the membrane-spanning F0 and the soluble F1 sectors, both of which are multiple protein complexes.
IF1 is a basic amphiphilic mitochondrial protein composed of 81 amino acids with a significant degree of homology in various species. This protein is encoded by the nuclear ATPIF1 gene. The gene ATPIF1 lies on the chromosome 1 and it is evolutionarily conserved throughout all eukaryotes, from yeast to mammals.
IF1 is mainly located within the mitochondrial matrix. The expression of IF1 in different normal tissues has been shown to vary largely, from very high levels in the heart, to intermediate expression in the liver and negligible levels in breast, colon and lung. IF1 can switch between two different states: an active dimeric form and an inactive tetrameric form, depending on the pH. IF1 forms a dimer at acidic pH (~6.7) and exhibits inhibitory effect, on the other hand, the tetrameric form, which is formed at basic pH (~8.0), cannot interact with ATP synthase.
IF1 has the unique capacity to inhibit, through a non-competitive mechanism, the adenosine triphosphate (ATP)-hydrolyzing activity of the F1F0-ATPsynthase without affecting the synthesis of ATP during oxidative phosphorylation. When mitochondria lose proton motive force, the interior of the mitochondria becomes acidic and IF1 reversibly binds to ATP synthase to block wasteful ATP consumption.
Under conditions of oxygen deprivation, such as during ischemia or in the presence of an uncoupler of oxidative phosphorylation, the F1F0-ATP synthase can switch from an ATP synthase to an ATPase, hydrolyzing ATP produced in the cytosol by glycolysis. To preserve ATP, C-terminal α-helix of IF1 is inserted into the interface between the α- and β-subunits of F1-ATPase and inhibits ATP hydrolysis.
Under aerobic conditions, whether IF1 has a role or what role IF1 plays in the control of the mitochondrial F1F0-ATP synthase/ATPase activity remains poorly understood. IF1 overexpression increased the activity of F1F0-ATP synthase by facilitation of dimerization of F1F0-ATP synthase in aerobic cell culture.
IF1 could play an important role in pathology of tissue ischemia and tumor growth by helping to conserve ATP under conditions of oxygen deprivation. Elevated expression is observed in a number of human cancers, including colon, lung, breast and ovarian cancers and hepatocellular carcinoma (HCC). Immunochemical determination of the amount of the natural ATPase inhibitor revealed that the tumor mitochondria contain 2-3 times more ATPase inhibitor than control mitochondria. It is concluded that the low ATPase activity of the tumor mitochondria results from the inhibition of the enzyme activity by the natural ATPase inhibitor.
Recent study reported that reciprocal activation between IF1 and nuclear factor NF-κB promoted HCC angiogenesis and metastasis. In colon cancer cells, IF1 promoted aerobic glycolysis and reactive oxygen species-mediated signaling pathway to enhance cell proliferation and cell survival. IF1 may promote tumor progression by promoting migration and invasion in glioma cells.

References to Summary

References to ATPase Inhibitor Mitochondrial

  • Faccenda D, Tan CH, Seraphim A, Duchen MR, Campanella M. IF1 limits the apoptotic-signalling cascade by preventing mitochondrial remodelling. Cell Death Differ. 2013 May;20 (5):686-97
  • Garcia-Bermudez J, Sanchez-Arago M, Soldevilla B, Del Arco A, Nuevo-Tapioles C, Cuezva JM. PKA Phosphorylates the ATPase Inhibitory Factor 1 and Inactivates Its Capacity to Bind and Inhibit the Mitochondrial H(+)-ATP Synthase. Cell Rep. 2015 Sep 29;12 (12):2143-55
  • Genoux A, Pons V, Radojkovic C, Roux-Dalvai F, Combes G, Rolland C, Malet N, Monsarrat B, Lopez F, Ruidavets JB, Perret B, Martinez LO. Mitochondrial inhibitory factor 1 (IF1) is present in human serum and is positively correlated with HDL-cholesterol. PLoS One. 2011;6 (9):e23949
  • Green DW, Grover GJ. The IF(1) inhibitor protein of the mitochondrial F(1)F(0)-ATPase. Biochim Biophys Acta. 2000 May 31;1458 (2-3):343-55
  • Guerrieri F, Scarfo R, Zanotti F, Che YW, Papa S. Regulatory role of the ATPase inhibitor protein on proton conduction by mitochondrial H+-ATPase complex. FEBS Lett. 1987 Mar 9;213 (1):67-72
  • Luciakova K, Kuzela S. Increased content of natural ATPase inhibitor in tumor mitochondria. FEBS Lett. 1984 Nov 5;177 (1):85-8
  • Moser TL, Kenan DJ, Ashley TA, Roy JA, Goodman MD, Misra UK, Cheek DJ, Pizzo SV. Endothelial cell surface F1-F0 ATP synthase is active in ATP synthesis and is inhibited by angiostatin. Proc Natl Acad Sci U S A. 2001 Jun 5;98 (12):6656-61
  • Nakamura J, Fujikawa M, Yoshida M. IF1, a natural inhibitor of mitochondrial ATP synthase, is not essential for the normal growth and breeding of mice. Biosci Rep. 2013;33 (5)
  • Runswick MJ, Bason JV, Montgomery MG, Robinson GC, Fearnley IM, Walker JE. The affinity purification and characterization of ATP synthase complexes from mitochondria. Open Biol. 2013 Feb;3 (2):120160
  • Sanchez-Arago M, Formentini L, Garcia-Bermudez J, Cuezva JM. IF1 reprograms energy metabolism and signals the oncogenic phenotype in cancer. Cell Cycle. 2012 Aug 15;11 (16):2963-4
  • Sanchez-Cenizo L, Formentini L, Aldea M, Ortega AD, Garcia-Huerta P, Sanchez-Arago M, Cuezva JM. Up-regulation of the ATPase inhibitory factor 1 (IF1) of the mitochondrial H+-ATP synthase in human tumors mediates the metabolic shift of cancer cells to a Warburg phenotype. J Biol Chem. 2010 Aug 13;285 (33):25308-13
  • Shen L, Zhi L, Hu W, Wu MX. IEX-1 targets mitochondrial F1Fo-ATPase inhibitor for degradation. Cell Death Differ. 2009 Apr;16 (4):603-12
  • Wu J, Shan Q, Li P, Wu Y, Xie J, Wang X. ATPase inhibitory factor 1 is a potential prognostic marker for the migration and invasion of glioma. Oncol Lett. 2015 Oct;10 (4):2075-2080
Related Products Documents