ECHS1 Antibody [N10G4] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:2000-1:20000 IP1:900-1:7500 IHC1:50-1:1000 IF1:400-1:1600

Application
WB, IP, IHC, IF

Reactivity
Human

Source
Mouse Monoclonal Antibody

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

Predicted MW Observed MW
31 kDa 31 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
ECHS1 Antibody [N10G4] detects endogenous levels of total ECHS1 protein.

Clone
N10G4

Synonym(s)
Enoyl-CoA hydratase, mitochondrial, mECH, mECH1, Enoyl-CoA hydratase 1 (ECHS1), Short-chain enoyl-CoA hydratase, SCEH

Background
ECHS1, or mitochondrial short-chain enoyl-CoA hydratase 1, serves as a core enzyme in the fatty acid β-oxidation spiral and branched-chain amino acid catabolism, particularly valine degradation, within the crotonase superfamily. The protein forms a compact barrel-like structure with a Rossmann fold for CoA ester binding and catalytic His-Asp dyad for proton abstraction, enabling stereospecific hydration of trans-2-enoyl-CoA thioesters. It catalyzes the second step of β-oxidation by adding water across the α-β double bond of medium- and short-chain enoyl-CoA (C4-C16) to generate L-3-hydroxyacyl-CoA, feeding downstream hydroxyacyl-CoA dehydrogenase and thiolase for acetyl-CoA production that enters the TCA cycle. High specificity targets methacrylyl-CoA from valine (yielding 2-methyl-3-hydroxybutyryl-CoA) and crotonyl-CoA from isoleucine/butyrate, though tiglyl-CoA binds without efficient turnover; multifunctional activity also handles leucine's 3-methylcrotonyl-CoA. Expressed ubiquitously but enriched in high-energy tissues like heart, muscle, and brain, ECHS1 maintains mitochondrial bioenergetics by linking lipid/amino acid oxidation to OXPHOS, with palmitate loading unmasking short-chain defects via butyrylcarnitine accumulation. Deficiency blocks these pathways, elevating toxic acryloyl-CoA/methacryloyl-CoA and 2-methyl-2,3-dihydroxybutyric acid in urine, secondary OXPHOS complex reductions (I/II/IV), lactate elevation, and Leigh-like basal ganglia lesions with cardiomyopathy, epilepsy, and encephalopathy. Patient fibroblasts show diminished protein/activity, while structural variants disrupt active site or tetramerization, linking to mitochondrial encephalopathy treatable potentially via metabolic interventions.

Background

ECHS1, or mitochondrial short-chain enoyl-CoA hydratase 1, serves as a core enzyme in the fatty acid β-oxidation spiral and branched-chain amino acid catabolism, particularly valine degradation, within the crotonase superfamily. The protein forms a compact barrel-like structure with a Rossmann fold for CoA ester binding and catalytic His-Asp dyad for proton abstraction, enabling stereospecific hydration of trans-2-enoyl-CoA thioesters. It catalyzes the second step of β-oxidation by adding water across the α-β double bond of medium- and short-chain enoyl-CoA (C4-C16) to generate L-3-hydroxyacyl-CoA, feeding downstream hydroxyacyl-CoA dehydrogenase and thiolase for acetyl-CoA production that enters the TCA cycle. High specificity targets methacrylyl-CoA from valine (yielding 2-methyl-3-hydroxybutyryl-CoA) and crotonyl-CoA from isoleucine/butyrate, though tiglyl-CoA binds without efficient turnover; multifunctional activity also handles leucine's 3-methylcrotonyl-CoA. Expressed ubiquitously but enriched in high-energy tissues like heart, muscle, and brain, ECHS1 maintains mitochondrial bioenergetics by linking lipid/amino acid oxidation to OXPHOS, with palmitate loading unmasking short-chain defects via butyrylcarnitine accumulation. Deficiency blocks these pathways, elevating toxic acryloyl-CoA/methacryloyl-CoA and 2-methyl-2,3-dihydroxybutyric acid in urine, secondary OXPHOS complex reductions (I/II/IV), lactate elevation, and Leigh-like basal ganglia lesions with cardiomyopathy, epilepsy, and encephalopathy. Patient fibroblasts show diminished protein/activity, while structural variants disrupt active site or tetramerization, linking to mitochondrial encephalopathy treatable potentially via metabolic interventions.

References
https://pubmed.ncbi.nlm.nih.gov/40446940/ https://pubmed.ncbi.nlm.nih.gov/26000322/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%