ACOX1 Antibody(C-term)

ACOX1 Antibody(C-term)
Cat.#: T0816
Rabbit Polyclonal Antibody
Clone ID: polyclonal
Swiss Prot: Q15067
Mol Weight: 74kDa
Size: 100ug

Description
ACOX1 is the first enzyme of the fatty acid beta-oxidation pathway, which catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. It donates electrons directly to molecular oxygen, thereby producing hydrogen peroxide. Defects in this gene result in pseudoneonatal adrenoleukodystrophy, a disease that is characterized by accumulation of very long chain fatty acids.

Recommended Applications
WB, ELISA

Applications and Recommended Dilution Factors
WB: 1:50~100
ELISA: 1:1,000

Species Reactivity
Human

Products Data

Western blot analysis of ACOX1 (arrow) using rabbit polyclonal ACOX1 Antibody (C-term) (RB04651). 293 cell lysates (2 ug/lane) either nontransfected (Lane 1) or transiently transfected with the ACOX1 gene (Lane 2) (Origene Technologies).

Specificity
This ACOX1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 631~660 amino acids from the C-terminal region of human ACOX1.

Storage Condition and Buffer
Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.

Alternative Names
ACOX1 antibody, ACOX antibody, MGC1198 antibody, PALMCOX antibody, SCOX antibody, Peroxisomal acyl-coenzyme A oxidase 1 antibody, Palmitoyl-CoA oxidase antibody, Straight-chain acyl-CoA oxidase antibody

Description References
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
Chu, R., et al., J. Biol. Chem. 270(9):4908-4915 (1995).
Aoyama, T., et al., Biochem. Biophys. Res. Commun. 198(3):1113-1118 (1994).
Fournier, B., et al., J. Clin. Invest. 94(2):526-531 (1994).
Varanasi, U., et al., Proc. Natl. Acad. Sci. U.S.A. 91(8):3107-3111 (1994).