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S5395

Superoxide Dismutase from bovine erythrocytes

BioReagent, ≥3,000 units/mg protein, suitable for cell culture, lyophilized powder

Synonim(y):

SOD, Superoxide: superoxide oxidoreductase

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Do Państwa/SKUDostępnośćCena netto
15000 units
Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności
721,00 zł
30000 units
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1310,00 zł
75000 units
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2430,00 zł

Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.75
EC Number:
232-943-0
MDL number:
Specific activity:
≥3,000 units/mg protein
Biological source:
bovine erythrocytes

721,00 zł


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biological source

bovine erythrocytes

Quality Segment

product line

BioReagent

form

lyophilized powder

specific activity

≥3,000 units/mg protein

mol wt

32.5 kDa

packaging

pkg of 15000 units

technique(s)

cell culture | mammalian: suitable

pH

7.6-10.5

shipped in

dry ice

storage temp.

−20°C

General description

Superoxide Dismutase from bovine erythrocytes is a metalloprotein which disproportionates superoxide anion radicals. It is a 31.5 kDa copper binding protein and displays a conserved domain and fold. It is a homodimer with one copper and zinc ion per subunit and has antiparallel “greek-key” β barrel fold.

Application

Superoxide Dismutase (SOD) from bovine erythrocytes has been used:
  • for measuring the superoxide radical using the electron paramagnetic resonance spin in human brain microvascular endothelial cells
  • for measuring superoxide production in cytochrome C assay in peripheral blood mononuclear cells
  • as a standard in characterization of hen egg SOD using Fourier-transform infrared spectroscopy (FTIR) and matrix-assisted laser desorption/ionization (MALDI) analysis

Biochem/physiol Actions

Superoxide Dismutase from bovine erythrocytes catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It serves as an antioxidant and plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.

Analysis Note

For assay method, see McCord, J.M. and Fridovich,I., J. Biol. Chem., 244, 6049 (1969).

Other Notes

One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 mL reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.
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S7571S9636S7446
technique(s)

cell culture | mammalian: suitable

technique(s)

immunoblotting: suitable, inhibition assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

specific activity

≥3,000 units/mg protein

specific activity

≥3,000 units/mg protein

specific activity

≥2,500 units/mg protein

specific activity

≥4,500 units/mg protein

biological source

bovine erythrocytes

biological source

bovine

biological source

human erythrocytes

biological source

-

form

lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

mol wt

32.5 kDa

mol wt

32.5 kDa

mol wt

32.0 kDa

mol wt

32.5 kDa

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

-


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Klasa składowania

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Questions

  1. I have purchased this item recently. I'd like to test it in a cell culture medium we're developing. I was wondering what buffer I should reconstitute the protein in and whether this buffer would be appropriate for long-term frozen storage?

    1 answer
    1. The buffer recommended to reconstitute this product is 0.1 M potassium phosphate, pH 7.5. The stock solution may be stored at –20 °C. This information is available in the product datasheet.

      Please see the link below to review this, as well as additional information.
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/320/129/s5395dat.pdf

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