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Mouse Anti-Porcine Squalene Epoxidase (SQLE) Monoclonal Antibody

Cat. No.VD8N333

Product TypeAnimal-targeted Antibodies

Size

Product Overview

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

Specifications

Application WB; IF; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G7N8
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Squalene Epoxidase
Isotype IgG2
Immunogen Recombinant protein of squalene epoxidase
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 squalene epoxidase (SQLE) is a key enzyme involved in the cholesterol biosynthesis pathway in pigs. SQLE catalyzes the conversion of squalene to 2,3-oxidosqualene, which is a critical step in the production of cholesterol and other sterols. This enzyme is located in the endoplasmic reticulum and plays a central role in the regulation of cholesterol homeostasis within cells. Cholesterol is an essential component of cell membranes, and it is also required for the synthesis of steroid hormones, bile acids, and vitamin D. SQLE's activity is tightly regulated to ensure that the cellular demand for cholesterol is met without causing an accumulation that could lead to detrimental effects.

Target Squalene Epoxidase
Target Synonym ERG1
Gene ID 100113409
UniProt ID A7L861

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. Padyana, Anil K., et al. "Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase." Nature communications 10.1 (2019): 97.
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