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Xanthine Oxidase Antibody
Rabbit Polyclonal
200-4183
200-4183S
200-4183-0100
50 mg
25 µL
100 µg
Lyophilized
Liquid (sterile filtered)
Lyophilized
WB, ELISA
Bovine
Rabbit
Shipping info:
$50.00 to US & $70.00 to Canada for most products. Final costs are calculated at checkout.
Product Details
Anti-Xanthine Oxidase (Buttermilk) (RABBIT) Antibody (BULK ORDER) - 200-4183
rabbit anti-Xanthine Oxidase Antibody, Xanthine dehydrogenase antibody, Xanthine dehydrogenase/oxidase antibody, Xanthine oxidase antibody, Xanthine oxidoreductase antibody, xdh antibody, xdha antibody, XO antibody, xor antibody
Rabbit
Polyclonal
IgG
Target Details
XDH - View All XDH Products
Bovine
Native Protein
Xanthine Oxidase [Bovine Buttermilk]
Anti-Xanthine Oxidase is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer stated above. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum as well as purified and partially purified Xanthine Oxidase [Bovine Buttermilk]. Cross reactivity against Xanthine Oxidase from other tissues and species may occur but have not been specifically determined.
Application Details
ELISA, WB
Xanthine Oxidase antibody has been tested by ELISA and western blot and is assayed against 1.0 ug of Xanthine Oxidase [Bovine Buttermilk] in a standard ELISA using Peroxidase conjugated Affinity Purified anti-Rabbit IgG [H&L] (Goat) code #611-1302 and (ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a substrate for 30 minutes at room temperature. A working dilution of 1:20,000 to 1:100,000 of the reconstitution concentration is suggested for this product.
Formulation
10.0 mg/mL by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
0.01% (w/v) Sodium Azide
None
5.0 mL
Restore with deionized water (or equivalent)
Shipping & Handling
Ambient
Store vial at 4° C prior to restoration. For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
Expiration date is one (1) year from date of receipt.
Xanthine dehydrogenase/oxidase is a key enzyme in purine degradation. It catalyzes the oxidation of hypoxanthine to xanthine. It catalyzes the oxidation of xanthine to uric acid. It contributes to the generation of reactive oxygen species. Xanthine dehydrogenase/oxidase can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.