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Mouse Anti-Porcine Glutaminase Monoclonal Antibody

Cat. No.VD8N245

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for glutaminase. It is affinity purified by protein A. It can be applied to WB, IHC, IF/ICC, IF-P and ELISA assays of glutaminase.

Specifications

Application WB; IHC; IF/ICC; IF-P; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G5N58
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Glutaminase
Isotype IgG2
Immunogen Recombinant protein of glutaminase
Purification Protein A Purified
Concentration 1900 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 glutaminase (pGLS) is an enzyme that catalyzes the hydrolysis of glutamine into glutamate and ammonia, playing a key role in the regulation of glutamine metabolism in pigs. This enzyme is predominantly expressed in the liver, kidney, and small intestine, where it contributes to the maintenance of glutamate homeostasis and the production of essential nitrogen-containing compounds. pGLS is involved in various physiological processes, including the provision of nitrogen for the synthesis of nucleotides, proteins, and other biomolecules. It also plays a role in the detoxification of ammonia, which is crucial for the urea cycle and overall nitrogen excretion.

Target Glutaminase
Target Synonym GLS; KGA
Gene ID 399525
UniProt ID A0A4X1THT5

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C (up to 12 months) 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. Kvamme, Elling, et al. "Glutaminase from pig renal cortex: I. purification and general properties." Journal of Biological Chemistry 245.8 (1970): 1871-1877.
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