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Mouse Anti-ACADVL Recombinant Antibody (V2-179181) (CBMAB-A0438-YC)

Provided herein is a Mouse monoclonal antibody against Human Acyl-CoA Dehydrogenase Very Long Chain. The antibody can be used for immunoassay techniques, such as ELISA, IHC-P, WB.
See all ACADVL antibodies
Published Data
Fig. 1 SDS western blot immunodetection of ACAD9, VLCAD, subunits of oxidative phosphorylation complex I, II, III and V and loading control β-actin on two control (C1 and C2) and two VLCAD-deficient (VLCADD1 and VLCADD2) patient fibroblasts, after stable knockdown of scrambled RNA (shControl) and stable knockdown of ACAD9 (shACAD9).
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Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-179181
Antibody Isotype
IgG2b, κ
Application
ELISA, IHC-P, WB

Basic Information

Immunogen
ACADVL (NP_000009, 345 a.a. ~ 434 a.a) partial recombinant protein with GST tag.
Specificity
Human
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IHC3 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
PBS, pH 7.2
Buffer
PBS, pH7.4
Preservative
None
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
acyl-Coenzyme A dehydrogenase, very long chain
Introduction
ACADVL is targeted to the inner mitochondrial membrane where it catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in
Entrez Gene ID
37
UniProt ID
P49748
Alternative Names
Acyl-CoA Dehydrogenase Very Long Chain; Acyl-Coenzyme A Dehydrogenase, Very Long Chain; VLCAD; Very Long-Chain Specific Acyl-CoA Dehydrogenase, Mitochondrial; EC 1.3.8.9; EC 1.3.99; ACAD6; LCACD;
Function
Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains.
Biological Process
Energy derivation by oxidation of organic compounds
Epithelial cell differentiation
Fatty acid beta-oxidation
Fatty acid beta-oxidation using acyl-CoA dehydrogenase
IRE1-mediated unfolded protein response
Negative regulation of fatty acid biosynthetic process
Negative regulation of fatty acid oxidation
Regulation of cholesterol metabolic process
Response to cold
Temperature homeostasis
Cellular Location
Mitochondrion inner membrane
Isoform 2: Mitochondrion inner membrane
Involvement in disease
An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting.
PTM
S-nitrosylation at Cys-237 in liver improves catalytic efficiency.

Gaston, G., Gangoiti, J. A., Winn, S., Chan, B., Barshop, B. A., Harding, C. O., & Gillingham, M. B. (2020). Cardiac tissue citric acid cycle intermediates in exercised very long‐chain acyl‐CoA dehydrogenase‐deficient mice fed triheptanoin or medium‐chain triglyceride. Journal of inherited metabolic disease, 43(6), 1232-1242.

Van Calcar, S. C., Sowa, M., Rohr, F., Beazer, J., Setlock, T., Weihe, T. U., ... & Singh, R. H. (2020). Nutrition management guideline for very-long chain acyl-CoA dehydrogenase deficiency (VLCAD): an evidence-and consensus-based approach. Molecular Genetics and Metabolism.

Chen, T., Tong, F., Wu, X. Y., Zhu, L., Yi, Q. Z., Zheng, J., ... & Jiang, P. P. (2020). Novel ACADVL variants resulting in mitochondrial defects in long-chain acyl-CoA dehydrogenase deficiency. Journal of Zhejiang University-SCIENCE B, 21(11), 885-896.

Zieger, M., Keeler, A. M., Flotte, T. R., & ElMallah, M. K. (2019). AAV9 gene replacement therapy for respiratory insufficiency in very‐long chain acyl‐CoA dehydrogenase deficiency. Journal of inherited metabolic disease, 42(5), 870-877.

Yamada, K., & Taketani, T. (2019). Management and diagnosis of mitochondrial fatty acid oxidation disorders: focus on very-long-chain acyl-CoA dehydrogenase deficiency. Journal of human genetics, 64(2), 73-85.

Rovelli, V., Manzoni, F., Viau, K., Pasquali, M., & Longo, N. (2019). Clinical and biochemical outcome of patients with very long-chain acyl-CoA dehydrogenase deficiency. Molecular genetics and metabolism, 127(1), 64-73.

Watanabe, K., Yamada, K., Sameshima, K., & Yamaguchi, S. (2018). Two siblings with very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency suffered from rhabdomyolysis after l-carnitine supplementation. Molecular genetics and metabolism reports, 15, 121-123.

Hesse, J., Braun, C., Behringer, S., Matysiak, U., Spiekerkoetter, U., & Tucci, S. (2018). The diagnostic challenge in very-long chain acyl-CoA dehydrogenase deficiency (VLCADD). Journal of inherited metabolic disease, 41(6), 1169-1178.

Tucci, S. (2017). Very long‐chain acyl‐CoA dehydrogenase (VLCAD‐) deficiency–studies on treatment effects and long‐term outcomes in mouse models. Journal of Inherited Metabolic Disease: Official Journal of the Society for the Study of Inborn Errors of Metabolism, 40(3), 317-323.

Obaid, A., Nashabat, M., Alfadhel, M., Alasmari, A., Al Mutairi, F., Alswaid, A., ... & Eyaid, W. (2017). Clinical, biochemical, and molecular features in 37 saudi patients with very long chain acyl coa dehydrogenase deficiency. In JIMD Reports, Volume 40 (pp. 47-53). Springer, Berlin, Heidelberg.

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For research use only. Not intended for any clinical use.

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