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Mouse Anti-Porcine Argininosuccinate Lyase (ASL) Monoclonal Antibody

Cat. No.VD8N357

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for argininosuccinate lyase. It is affinity purified by protein A. It can be applied to WB and ELISA assays of argininosuccinate lyase.

Specifications

Application WB; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G8N10
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Argininosuccinate Lyase
Isotype IgG2
Immunogen Recombinant protein of argininosuccinate lyase
Purification Protein A Purified
Concentration 1000 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 argininosuccinate lyase (pASL) is an enzyme that plays a critical role in the urea cycle, a metabolic pathway responsible for the detoxification of ammonia in mammals. pASL catalyzes the conversion of argininosuccinate to arginine and fumarate, a reaction that is essential for the production of urea from ammonia and is a key step in maintaining nitrogen balance within the body. This enzyme is predominantly found in the liver, where it functions to mitigate the toxic effects of ammonia by incorporating it into the urea molecule, which can then be safely excreted. pASL is also present in other tissues, including the kidneys, where it may contribute to additional metabolic processes.

Target Argininosuccinate Lyase
Gene ID 100517757
UniProt ID A0A8D1NJT9

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. Zheng, Liang, et al. "Reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells." Cancer & metabolism 1 (2013): 1-11.
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