Datasheet

生物学的記述

Specificity	GRIM19 Antibody [J7L19] detects endogenous levels of total GRIM19 protein.
Background	GRIM19, also known as NDUFA13, serves as an integral nuclear-encoded subunit of mitochondrial complex I within the NADH:ubiquinone oxidoreductase assembly, essential for electron transfer from NADH to ubiquinone during oxidative phosphorylation and maintenance of mitochondrial membrane potential. The protein adopts a compact helical bundle structure anchored peripherally to the matrix arm of complex I, positioning its LYR motif to stabilize the Q-module and facilitate conformational coupling between FMN reduction and quinone binding pocket dynamics that drive proton pumping across the inner membrane. Upregulation by type I interferons and retinoic acid through IRF/STAT promoter elements recruits GRIM19 to antagonize STAT3 dimerization by direct binding to its phosphotyrosine tail, blocking nuclear translocation and transcriptional activation of survival genes like c-Myc and Bcl-xL while sensitizing cells to apoptosis via Bax oligomerization. GRIM19 coordinates iron-sulfur cluster relay from the N-module through conformational gating that prevents ROS leakage during reverse electron transport, intersecting with NLRP3 inflammasome regulation, where its depletion elevates mtROS to activate caspase-1 and gasdermin D pore formation, amplifying IL-1β/IL-33 secretion in macrophages and hepatocytes. Loss disrupts fetal hematopoietic stem cell differentiation and adult quiescence through SHP-1/TGF-β axis impairment, while in parietal cells, GRIM19 deficiency triggers ROS-NRF2-HO-1-NF-κB signaling to license NLRP3-dependent spasmolytic polypeptide-expressing metaplasia. Overexpression promotes brown adipose differentiation by shifting PPARγ coactivator-1α toward thermogenic programs, countering diet-induced obesity.

Specificity

GRIM19 Antibody [J7L19] detects endogenous levels of total GRIM19 protein.

Background

GRIM19, also known as NDUFA13, serves as an integral nuclear-encoded subunit of mitochondrial complex I within the NADH:ubiquinone oxidoreductase assembly, essential for electron transfer from NADH to ubiquinone during oxidative phosphorylation and maintenance of mitochondrial membrane potential. The protein adopts a compact helical bundle structure anchored peripherally to the matrix arm of complex I, positioning its LYR motif to stabilize the Q-module and facilitate conformational coupling between FMN reduction and quinone binding pocket dynamics that drive proton pumping across the inner membrane. Upregulation by type I interferons and retinoic acid through IRF/STAT promoter elements recruits GRIM19 to antagonize STAT3 dimerization by direct binding to its phosphotyrosine tail, blocking nuclear translocation and transcriptional activation of survival genes like c-Myc and Bcl-xL while sensitizing cells to apoptosis via Bax oligomerization. GRIM19 coordinates iron-sulfur cluster relay from the N-module through conformational gating that prevents ROS leakage during reverse electron transport, intersecting with NLRP3 inflammasome regulation, where its depletion elevates mtROS to activate caspase-1 and gasdermin D pore formation, amplifying IL-1β/IL-33 secretion in macrophages and hepatocytes. Loss disrupts fetal hematopoietic stem cell differentiation and adult quiescence through SHP-1/TGF-β axis impairment, while in parietal cells, GRIM19 deficiency triggers ROS-NRF2-HO-1-NF-κB signaling to license NLRP3-dependent spasmolytic polypeptide-expressing metaplasia. Overexpression promotes brown adipose differentiation by shifting PPARγ coactivator-1α toward thermogenic programs, countering diet-induced obesity.

使用情報

Application

WB

Dilution

WB

1:1000

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

16 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/15367666/
https://pubmed.ncbi.nlm.nih.gov/27659873/

Application Data

WB

Validated by Selleck

Lane 1: Daudi, Lane 2: TT, Lane 3: HepG2, Lane 4: VCaP