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Mouse Anti-Porcine Aminomethyltransferase (AMT) Monoclonal Antibody

Cat. No.VD8N360

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for aminomethyltransferase. It is affinity purified by protein G. It can be applied to WB, IF, IHC and ELISA assays of aminomethyltransferase.

Specifications

Application WB; IF; IHC; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G8N13
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Aminomethyltransferase
Isotype IgG1
Immunogen Recombinant protein of aminomethyltransferase
Purification Protein G Purified
Concentration 1500 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 aminomethyltransferase (pAMT) is an enzyme that catalyzes the transfer of an aminomethyl group from S-adenosylmethionine to acceptor molecules, a reaction that is integral to the biosynthesis of glycine and the activation of folate. This protein plays a pivotal role in one-carbon metabolism, which is essential for various biological processes, including DNA synthesis, methylation, and the production of certain amino acids. pAMT is highly conserved across species, reflecting its importance in maintaining cellular homeostasis. In pigs, this enzyme contributes to the metabolic pathways that support growth, development, and the overall health of the animal. Its activity is regulated by various factors, including the availability of substrates and the cellular demand for one-carbon units.

Target Aminomethyltransferase
Gene ID 396679
UniProt ID I3LIR4

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. Okamura-Ikeda, Kazuko, et al. "Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism." Journal of Biological Chemistry 285.24 (2010): 18684-18692.
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