Datasheet

生物学的記述

Specificity	ATPIF1 Antibody [P8F22] detects endogenous levels of total ATPIF1 protein.
Background	ATPIF1 (ATPase Inhibitory Factor 1, also IF1) is a small mitochondrial regulatory protein that physiologically inhibits the H+-ATP synthase (Complex V) to prevent ATP hydrolysis under conditions of impaired respiration or acidosis. ATPIF1 exists as an intrinsically disordered monomer in solution that undergoes disorder-to-order transition upon binding, forming two α-helices: an N-terminal helix inserting into the catalytic interface between αDP/βDP subunits of the F1 domain to sterically block rotary catalysis, and a C-terminal anti-parallel coiled-coil stabilizing IF1 homodimers. ATPIF1 binds pH-dependently to the F1 sector during ATP hydrolysis (not synthesis), locking the enzyme in the DP:IF1 conformation to preserve cellular ATP while promoting ATP synthase oligomerization (dimers/tetramers) that shapes cristae architecture and inhibits permeability transition pore (PTP) opening via OSCP subunit interaction. It triggers retrograde signaling, inducing aerobic glycolysis (Warburg effect) in cancer cells and modulates mitohormesis/apoptosis resistance. Overexpression in carcinomas drives oncogenesis, metabolic reprogramming, and tumor survival; deficiency disrupts cristae/mitochondrial structure, linking to pathologies like heart failure.

Specificity

ATPIF1 Antibody [P8F22] detects endogenous levels of total ATPIF1 protein.

Background

ATPIF1 (ATPase Inhibitory Factor 1, also IF1) is a small mitochondrial regulatory protein that physiologically inhibits the H+-ATP synthase (Complex V) to prevent ATP hydrolysis under conditions of impaired respiration or acidosis. ATPIF1 exists as an intrinsically disordered monomer in solution that undergoes disorder-to-order transition upon binding, forming two α-helices: an N-terminal helix inserting into the catalytic interface between αDP/βDP subunits of the F1 domain to sterically block rotary catalysis, and a C-terminal anti-parallel coiled-coil stabilizing IF1 homodimers. ATPIF1 binds pH-dependently to the F1 sector during ATP hydrolysis (not synthesis), locking the enzyme in the DP:IF1 conformation to preserve cellular ATP while promoting ATP synthase oligomerization (dimers/tetramers) that shapes cristae architecture and inhibits permeability transition pore (PTP) opening via OSCP subunit interaction. It triggers retrograde signaling, inducing aerobic glycolysis (Warburg effect) in cancer cells and modulates mitohormesis/apoptosis resistance. Overexpression in carcinomas drives oncogenesis, metabolic reprogramming, and tumor survival; deficiency disrupts cristae/mitochondrial structure, linking to pathologies like heart failure.

使用情報

Application

WB, IP, IHC, IF

Dilution

WB	IP	IHC	IF
1:1000	1:100	1:1600	1:3200

Reactivity

Human, Monkey

Source

Rabbit Monoclonal Antibody

MW

12 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/35620611/
https://pubmed.ncbi.nlm.nih.gov/38280428/

ATPIF1 Antibody [P8F22]

生物学的記述

使用情報

References

Application Data