Human Cu/ZnSOD ELISA Kit (48-well)

CAT#: EA100095

Human Cu/ZnSOD ELISA Kit (48-well)

Size: 1 x 48 wells 1 x 96 wells


USD 290.00

3 Weeks*

Size
    • 1 x 48 wells

Product Images

Other products for "SOD1"

Specifications

Product Data
Format 48-well strip plate
Assay Type Solid Phase Sandwich ELISA
Assay Length 3 hours
Signal Colorimetric
Curve Range 78-5000pg/ml
Sample Type Cell culture supernatant, serum, plasma (EDTA, citrate, heparin)
Sample Volume 20 uL
Specificity Natural and recombinant Human Cu/ZnSOD Ligand
Sensitivity 40pg/mL
Reactivities Human
Interference No significant interference observed with available related molecules.
Components
  • Aluminium pouches with a Microwell Plate coated with antibody to human Cu/ZnSOD (8X6)
  • 2 vials human Cu/ZnSOD Standard lyophilized, 2500 pg/ml upon reconstitution
  • 2 vials HRP-Conjugate solution
  • 4 bottle Standard /sample Diluent
  • 1 bottle HRP-Conjugate Diluent
  • 1 bottle Wash Buffer Concentrate 20x (PBS with 1% Tween-20)
  • 1 vial Substrate Solution
  • 1 vial Stop Solution
  • 4 pieces Adhesive Films
  • package insert
Background

Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturallyoccuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 1, SOD1, also known as Cu/Zn SOD, soluble SOD and IPOA, is a soluble, cytoplasmic 16 kDa homodimer. Each SOD1 monomer binds one Cu2+ and one Zn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD1 shares 23% and 27% sequence identity with SOD2 and SOD3, respectively. Mutations in SOD1 have been implicated as causes of familial amyotrophic lateral sclerosis (ALS). The ALScausing mutations of SOD1 are scattered throughout the protein and provide no clear functional or structural clues to the underlying disease mechanism. The oligomerization hypothesis suggests that mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight aggregates that result in the death of motor neurons. The oxidative damage hypothesis suggests that loss of function mutation in SOD1 protein results in the accumulation of cellular superoxide radical, leading to free radicalmediated damage, the release of cytochrome c, and apoptosis.

Gene Symbol SOD1
Standard Curve
Representative standard curve for Cu/ZnSOD ELISA. Cu/ZnSOD was diluted in serial two-fold steps in Sample Diluent.

Documents

{0} Product Review(s)

0 Product Review(s) Submit review

Be the first one to submit a review

Product Citations

*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.