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AB110299

Anti-EHHADH 抗体 [7F6AF11]

Anti-EHHADH antibody [7F6AF11]

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(1 Publication)

Mouse Monoclonal EHHADH antibody. Suitable for ICC, IP and reacts with Human samples. Cited in 1 publication.

別名を表示する

ECHD, EHHADH, Peroxisomal bifunctional enzyme, PBE, PBFE, L-bifunctional protein, Multifunctional enzyme 1, LBP, MFE1

2 Images
Immunocytochemistry - Anti-EHHADH antibody [7F6AF11] (AB110299)
  • ICC

Unknown

Immunocytochemistry - Anti-EHHADH antibody [7F6AF11] (AB110299)

Immunocytochemistry image of EHHADH stained Human HepG2 cells. The cells were paraformaldehyde fixed (4%, 20 min) and Triton X-100 permeabilized (0.1%, 15min). The cells were incubated ab110299 at 1µg/ml for 2h at room temperature or over night at 4°C. The secondary antibody was (red) Alexa Fluor® 594 goat anti-mouse IgG (H+L) used at a 1/1000 dilution for 1h. 10% Goat serum was used as the blocking agent for all blocking steps. DAPI was used to stain the cell nuclei (blue). Target protein locates mainly in peroxisome.

Immunoprecipitation - Anti-EHHADH antibody [7F6AF11] (AB110299)
  • IP

Unknown

Immunoprecipitation - Anti-EHHADH antibody [7F6AF11] (AB110299)

Immonprecipitation analysis of enriched subcellular organelles from human liver, which contains mitochondria and peroxisome. EHHADH immunocaptured using ab110299.

All lanes:

Immunoprecipitation - Anti-EHHADH antibody [7F6AF11] (ab110299)

Predicted band size: 79 kDa

false

Key facts

宿主種

Mouse

クローン性

Monoclonal

クローン番号

7F6AF11

アイソタイプ

IgG3

軽鎖のタイプ

kappa

キャリアフリー

No

交差種

Human

アプリケーション

IP, ICC

applications

免疫原

The exact immunogen used to generate this antibody is proprietary information.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ICC" : {"fullname" : "Immunocytochemistry", "shortname":"ICC"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ICC-species-checked": "testedAndGuaranteed", "ICC-species-dilution-info": "1 µg/mL", "ICC-species-notes": "<p></p>", "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "", "IP-species-notes": "<p></p>" } } }
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製品の詳細

Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com
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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Proprietary technique
精製に関する特記事項
Near homogeneity as judged by SDS-PAGE (>95% purity). The antibody was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation.
バッファー組成
pH: 7.5 Preservative: 0.02% Sodium azide Constituents: HEPES buffered saline
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
+4°C
保管に関する情報
Do Not Freeze
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補足情報

This supplementary information is collated from multiple sources and compiled automatically.

EHHADH also known as enoyl-CoA hydratase/3-hydroxyacyl CoA dehydrogenase is a mitochondrial enzyme. Its molecular mass is approximately 82 kDa. EHHADH catalyzes two sequential reactions in the β-oxidation of fatty acids converting L-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. This enzyme expresses mainly in liver and kidney tissues playing a role in lipid metabolism.
Biological function summary

EHHADH acts within the peroxisome a cellular organelle that facilitates lipid metabolism and detoxification processes. EHHADH is a part of the mitochondrial trifunctional protein complex. This complex helps in breaking down long-chain fatty acids highlighting EHHADH's role in energy production.

Pathways

EHHADH engages in the fatty acid β-oxidation pathway and the peroxisomal fatty acid β-oxidation pathway. In these pathways EHHADH works alongside proteins like HADHA and HADHB both of which are part of the trifunctional protein complex. The collaboration between these proteins ensures efficient lipid degradation and energy release.

EHHADH links to disorders such as peroxisomal biogenesis disorders and Zellweger syndrome. Mutations affecting EHHADH or its associated proteins like VLCAD (very-long-chain acyl-CoA dehydrogenase) can disrupt normal mitochondrial functions. This disruption can lead to accumulation of unmetabolized fatty acids contributing to disease progression.
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製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:
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ターゲットの情報

Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed : 15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (PubMed : 15060085).
See full target information EHHADH
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文献 (1)

Recent publications for all applications. Explore the full list and refine your search

Autophagy :1-15 PubMed31964216

2020

Loss of HSPA9 induces peroxisomal degradation by increasing pexophagy.

Applications

Unspecified application

Species

Unspecified reactive species

Doo Sin Jo,So Jung Park,Ae-Kyeong Kim,Na Yeon Park,Joon Bum Kim,Ji-Eun Bae,Hyun Jun Park,Ji Hyun Shin,Jong Wook Chang,Peter K Kim,Yong-Keun Jung,Jae-Young Koh,Seong-Kyu Choe,Kyu-Sun Lee,Dong-Hyung Cho
View all publications
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