Rabbit Anti-Human HADHA (a.a. 31-763) Polyclonal antibody

Name: Rabbit Anti-Human HADHA (a.a. 31-763) Polyclonal antibody
SKU: DPABH-26401
Rating: 5 (1 reviews)

Rabbit Anti-Human HADHA (a.a. 31-763) Polyclonal antibody for ELISA, IHC, WB

COA

SDS

Datasheet

Key features and details

Target: Human HADHA
Host: Rabbit
Application: ELISA, IHC, WB
Species Reactivity: Human

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

E. coli - derived recombinant Human HADHA (Gly31-Gln763).

Conjugate

Unconjugated

Applications

Application Notes

ELISA: 1:4000-1:8000
IHC: 1:50-1:100
WB: 1:1000-1:4000

General Notes

This product (Catalog No. DPABH-26401) is a rabbit-derived polyclonal antibody raised against human HADHA, targeting the amino acid region 31–763 of the protein. It has been affinity purified by Protein A. HADHA is a human gene that encodes the alpha subunit of the mitochondrial trifunctional protein (MTP), an enzyme complex critical for catalyzing the final three steps of beta-oxidation of long-chain fatty acids in mitochondria, thereby facilitating energy production from fats. The HADHA gene is located on the short arm of chromosome 2 at position 2p23.3, spanning approximately 54 kilobases with 20 exons, and it is oriented head-to-head with the adjacent HADHB gene, which encodes the beta subunit of MTP. The resulting alpha subunit protein, also known as trifunctional enzyme subunit alpha, mitochondrial, consists of 763 amino acids and possesses two key enzymatic activities: long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) and long-chain enoyl-CoA hydratase, which work in concert with the beta subunit's thiolase activity to break down fatty acids into acetyl-CoA for the citric acid cycle.
DPABH-26401 is suitable for use in ELISA (1:4,000–1:8,000), IHC (1:50–1:100), Western blot (WB) (1:1,000–1:4,000) applications.
DPABH-26401 is supplied as a liquid formulation in 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

78 kDa gastrin-binding protein; HADH; HADHA; Trifunctional enzyme subunit alpha; mitochondrial; TP-alpha; Monolysocardiolipin acyltransferase

UniProt ID

P40939

Citations

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Documents

pdf COA

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pdf Datasheet

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Customer Reviews

References

Mutations in HADHB, which Encodes the b- Subunit of Mitochondrial Trifunctional Protein, Cause Infantile Onset Hypoparathyroidism and Peripheral Polyneuropathy

AMERICAN JOURNAL OF MEDICAL GENETICS PART A

Authors: Naiki, Misako; Ochi, Nobuhiko; Kato, Yusuke S.; Purevsuren, Jamiyan; Yamada, Kenichiro; Kimura, Reiko; Fukushi, Daisuke; Hara, Shinya; Yamada, Yasukazu; Kumagai, Toshiyuki; Yamaguchi, Seiji; Wakamatsu, Nobuaki

Abstract

Mitochondrial trifunctional protein (MTP) is a hetero-octamer composed of four - and four -subunits that catalyzes the final three steps of mitochondrial -oxidation of long chain fatty acids. HADHA and HADHB encode the -subunit and the -subunit of MTP, respectively. To date, only two cases with MTP deficiency have been reported to be associated with hypoparathyroidism and peripheral polyneuropathy. Here, we report on two siblings with autosomal recessive infantile onset hypoparathyroidism, peripheral polyneuropathy, and rhabdomyolysis. Sequence analysis of HADHA and HADHB in both siblings shows that they were homozygous for a mutation in exon 14 of HADHB (c.1175C>T, [p.A392V]) and the parents were heterozygous for the mutation. Biochemical analysis revealed that the patients had MTP deficiency. Structural analysis indicated that the A392V mutation identified in this study and the N389D mutation previously reported to be associated with hypoparathyroidism are both located near the active site of MTP and affect the conformation of the -subunit. Thus, the present patients are the second and third cases of MTP deficiency associated with missense HADHB mutation and infantile onset hypoparathyroidism. Since MTP deficiency is a treatable disease, MTP deficiency should be considered when patients have hypoparathyroidism as the initial presenting feature in infancy. (c) 2014 Wiley Periodicals, Inc.

Metabolic Reprogramming in Amyotrophic Lateral Sclerosis

SCIENTIFIC REPORTS

Authors: Szelechowski, M.; Amoedo, N.; Obre, E.; Leger, C.; Allard, L.; Bonneu, M.; Claverol, S.; Lacombe, D.; Oliet, S.; Chevallier, S.; Le Masson, G.; Rossignol, R.

Abstract

Mitochondrial dysfunction in the spinal cord is a hallmark of amyotrophic lateral sclerosis (ALS), but the neurometabolic alterations during early stages of the disease remain unknown. Here, we investigated the bioenergetic and proteomic changes in ALS mouse motor neurons and patients' skin fibroblasts. We first observed that SODG93A mice presymptomatic motor neurons display alterations in the coupling efficiency of oxidative phosphorylation, along with fragmentation of the mitochondrial network. The proteome of presymptomatic ALS mice motor neurons also revealed a peculiar metabolic signature with upregulation of most energy-transducing enzymes, including the fatty acid oxidation (FAO) and the ketogenic components HADHA and ACAT2, respectively. Accordingly, FAO inhibition altered cell viability specifically in ALS mice motor neurons, while uncoupling protein 2 (UCP2) inhibition recovered cellular ATP levels and mitochondrial network morphology. These findings suggest a novel hypothesis of ALS bioenergetics linking FAO and UCP2. Lastly, we provide a unique set of data comparing the molecular alterations found in human ALS patients' skin fibroblasts and SODG93A mouse motor neurons, revealing conserved changes in protein translation, folding and assembly, tRNA aminoacylation and cell adhesion processes.