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Mouse Anti-Porcine 4-Hydroxyphenylpyruvate Dioxygenase (HPD) Monoclonal Antibody

Cat. No.VD8N411

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for 4-hydroxyphenylpyruvate dioxygenase. It is affinity purified by protein A. It can be applied to WB, IHC and ELISA assays of 4-hydroxyphenylpyruvate dioxygenase.

Specifications

Application WB; IHC; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G9N11
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity 4-Hydroxyphenylpyruvate Dioxygenase
Isotype IgG2
Immunogen Recombinant protein of 4-hydroxyphenylpyruvate dioxygenase
Purification Protein A Purified
Concentration 2000 μg/mL
Conjugation Unconjugated
Preservative and Stabilizer 0.02% Sodium Azide
Buffer Phosphate Buffered Saline with 50% Glycerol, pH 7.3
Physical State Liquid

Target Information

Porcine 4-Hydroxyphenylpyruvate Dioxygenase (pHPPD) is an enzyme that plays a critical role in the tyrosine catabolic pathway in pigs. This enzyme is responsible for the conversion of 4-hydroxyphenylpyruvate (HPP) to homogentisate, a reaction that involves the incorporation of molecular oxygen and the subsequent degradation of homogentisate to fumarate and acetoacetate. pHPPD is a member of the non-heme iron-dependent dioxygenase family, which means it requires an iron ion for its catalytic activity. The enzyme's function is essential for maintaining tyrosine homeostasis and preventing the accumulation of its metabolites, which can be toxic.

Target 4-Hydroxyphenylpyruvate Dioxygenase
Target Synonym 4 HPPD; 4HPPD
Gene ID 397443
UniProt ID Q02110

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C on receipt.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Raspail, Corinne, et al. "4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme." Journal of Biological Chemistry 286.29 (2011): 26061-26070.
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