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Superoxide Dismutase (Cu/Zn Enzyme) Antibody

$995.00

Catalog Number: B2010585 (100 uL)
Superoxide Dismutase (Cu/Zn Enzyme) Antibody is specific to Cu/Zn SOD (does not cross-react with Mn SOD). This product has been used as molecular tool in the study of SOD. It has also been used in a wide array of other biochemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

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SKU: B2010585 Category:

Description

Superoxide Dismutase (Cu/Zn Enzyme) Antibody
Catalog number: B2010585
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 100 uL
Molecular Weight or Concentration: na
Supplied as: Purified Antibody
Applications: molecular tool in the study of SOD
Storage: -20C
Keywords: Anti-SOD, Anti-Superoxide Dismutase
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: M Fetherolf M, Boyd SD, Winkler DD, Winge DR. Oxygen-dependent activation of
Cu,Zn-superoxide dismutase-1. Metallomics. 2017 Aug 16;9(8):1047-1059.

2: Eleutherio ECA, Silva Magalhães RS, de Araújo Brasil A, Monteiro Neto JR, de
Holanda Paranhos L. SOD1, more than just an antioxidant. Arch Biochem Biophys.
2021 Jan 15;697:108701.

3: Deepa SS, Van Remmen H, Brooks SV, Faulkner JA, Larkin L, McArdle A, Jackson
MJ, Vasilaki A, Richardson A. Accelerated sarcopenia in Cu/Zn superoxide
dismutase knockout mice. Free Radic Biol Med. 2019 Feb 20;132:19-23.

4: Anzai I, Tokuda E, Handa S, Misawa H, Akiyama S, Furukawa Y. Oxidative
misfolding of Cu/Zn-superoxide dismutase triggered by non-canonical
intramolecular disulfide formation. Free Radic Biol Med. 2020 Feb 1;147:187-199.

5: Chandrasekharan B, Montllor-Albalate C, Colin AE, Andersen JL, Jang YC, Reddi
AR. Cu/Zn Superoxide Dismutase (Sod1) regulates the canonical Wnt signaling
pathway. Biochem Biophys Res Commun. 2021 Jan 1;534:720-726.

6: Furukawa Y, Tokuda E. Does wild-type Cu/Zn-superoxide dismutase have
pathogenic roles in amyotrophic lateral sclerosis? Transl Neurodegener. 2020 Aug
19;9(1):33.

7: Pokrishevsky E, Nan J, Cashman NR. Induction of Cu/Zn Superoxide Dismutase
(SOD1) Aggregation in Living Cells. Methods Mol Biol. 2019;1873:213-224.

8: Paravani EV, Odetti LM, Simoniello MF, Poletta GL. Molecular analysis and
bioinformatic characterization of cooper, zinc-superoxide dismutase (Cu/Zn-sod)
gene of Caiman latirostris. Mol Biol Rep. 2020 Nov;47(11):8849-8857.

9: Bakavayev S, Chetrit N, Zvagelsky T, Mansour R, Vyazmensky M, Barak Z,
Israelson A, Engel S. Cu/Zn-superoxide dismutase and wild-type like fALS SOD1
mutants produce cytotoxic quantities of H2O2 via cysteine-
dependent redox short-circuit. Sci Rep. 2019 Jul 25;9(1):10826.
10: Tasaki E, Kobayashi K, Matsuura K, Iuchi Y. Long-Lived Termite Queens
Exhibit High Cu/Zn-Superoxide Dismutase Activity. Oxid Med Cell Longev. 2018 Feb
13;2018:5127251.

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