Superoxide Dismutase 1 Human Recombinant - 25µg

misc
miscmisc
Catalog #: PRO-648Description:Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having a total molecular mass of 15.9 kDa.The SOD1 is purified by proprietary chromatographic techniques.Synonyms:Supe ...Read more
Catalog # PRO-648 $225.00 each


100 items in stock
Add to cart
  • Description
  • Specifications

Catalog #: PRO-648

Description:
Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having a total molecular mass of 15.9 kDa.
The SOD1 is purified by proprietary chromatographic techniques.

Synonyms:
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

Source:
Escherichia Coli.

Amino Acid Sequence:
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ.

Purity:
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Formulation:
SOD1 0.2um filtered solution contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

Stability:
Store at 4 °C if entire vial will be used within 2-4 weeks. Store, frozen at -20 °C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.

Activity:
Specific activity is > 90 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25C in a 1.5 ml reaction volume.

Physical Appearance:
Sterile Filtered colorless solution.

Usage:
Denovo Biotechnology's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

We have 696 researchers online

Your Purchases

The cart is empty