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Mouse Anti-Porcine 3-Oxoacid CoA Transferase 1 (OXCT1) Monoclonal Antibody

Cat. No.VD8N387

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for 3-oxoacid coa transferase 1. It is affinity purified by protein G. It can be applied to WB, IHC, IF/ICC, FC and ELISA assays of 3-oxoacid coa transferase 1.

Specifications

Application WB; IHC; IF/ICC; FC; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G8N40
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity 3-Oxoacid CoA Transferase 1
Isotype IgG1
Immunogen Recombinant protein of 3-oxoacid coa transferase 1
Purification Protein G Purified
Concentration 500 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 3-oxoacid CoA transferase 1 (pOXCT1), also known as mitochondrial 3-oxoacyl-CoA thiolase, is a key enzyme involved in the mitochondrial fatty acid beta-oxidation pathway. This protein plays a crucial role in the breakdown of fatty acids to produce acetyl-CoA, which subsequently enters the citric acid cycle to generate ATP, the cell's primary energy currency. pOXCT1 is particularly important in tissues with high energy demands, such as the liver, heart, and skeletal muscle, where it contributes to the regulation of fatty acid metabolism. In pigs, this enzyme may be critical for supporting the energy needs during periods of growth, lactation, and physical activity.

Target 3-Oxoacid CoA Transferase 1
Target Synonym SCOT; OXCT
Gene ID 396978
UniProt ID Q29551

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. Shafqat, Naeem, et al. "A structural mapping of mutations causing succinyl-CoA: 3-ketoacid CoA transferase (SCOT) deficiency." Journal of inherited metabolic disease 36 (2013): 983-987.
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