Fructosyl-Amino Acid Oxidase [E.coli] Sheep Polyclonal Antibody

CAT#: R1147

Fructosyl-Amino Acid Oxidase [E.coli] sheep polyclonal antibody, Serum

Specifications

Product Data

• Applications: ELISA, IP, WB
• Recommended Dilution: Suitable for Immunoblotting (Western 1:500-1:5,000), ELISA, Immunoprecipitation (1:100) and most Immunological methods requiring high titer and specificity.
  Recommended Diutions: This product has been assayed against 1.0 µg of Fructosyl-Amino Acid Oxidase [E.coli] in a standard sandwich ELISA using Peroxidase conjugated Affinity Purified anti-Sheep IgG [H&L] (Rabbit) and (ABTS (2,2'-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) 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.
• Host: Sheep
• Clonality: Polyclonal
• Immunogen: Fructosyl-Amino Acid Oxidase [E.coli].
• Specificity: Assay by immunoelectrophoresis resulted in a single precipitin arc against purified and partially purified Fructosyl-Amino Acid Oxidase [E.coli].
  Cross reactivity against Fructosyl-Amino Acid Oxidase from other sources is unknown.
• Formulation: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01% sodium azide as preservative.
  State: Serum
  State: Lyophilized purified Ig fraction.
• Reconstitution Method: Restore with 2.0 ml of deionized water (or equivalent).
• Concentration: 90.0 mg/ml (by Refractometry)
• Purification: Prepared from monospecific antiserum by a delipidation and defibrination.
• Background: Fructosyl amino acid oxidase (FAOX or FAOD) catalyzes the oxidative deglycation of fructosyl amino acids, yielding the corresponding amino acid, glucosone, and hydrogen peroxide. Glucose can be attached to aminoacids by a nonenzymatic reaction called "glycation", to distinguish it from the enzymatic glycosylation of proteins.
  (FAOX) can be used for the enzymatic detection of nonenzymatically glycated proteins. Glycation of protein has been implicated in the development of diabetic complications and the aging process. Glycation of blood proteins such as hemoglobin and albumin is enhanced in diabetics with high blood glucose. The amounts of these glycated proteins reflect the level of blood glucose in periods corresponding to the half life of the protein (14 to 20 days for albumin and 1 to 2 months for hemoglobin). Since the glycation of blood proteins is not affected by transient increases in blood glucose, the levels of glycated proteins are good indices for monitoring diabetes mellitus patients during therapy. HbA1c, blood levels of which are a good index of the long term control of blood glucose in patients with diabetes mellitus, is defined as an amino end of the ß subunit (valine residue) of hemoglobin that has been glycated nonenzymatically.