Recombinant Human LIPA HA-tag His-tag Protein, CF

Recombinant Human LIPA HA-tag His-tag Protein, CF Summary

• R&D Systems CHO-derived Recombinant Human LIPA HA-tag His-tag Protein (11633-LA)
• Quality control testing to verify active proteins with lot specific assays by in-house scientists
• All R&D Systems proteins are covered with a 100% guarantee

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Assay Procedure

Background: LIPA

Recombinant human Lysosomal acid lipase (LAL) or Lipase A (LIPA), also known as acid cholesteryl ester hydrolase, is a 378 residue mature, glycosylated, lysosomal serine hydrolase of a family of three mammalian acid lipases. Mature LIPA contains a globular core domain typical of a/b hydrolase-fold family members and a cap domain. Beneath the cap region, the core domain contains the catalytic triad surrounded by a hydrophobic surface that promotes lipid substrate binding (1). Except for erythrocytes, LIPA is broadly expressed in cells (1) and is found in the lysozyme where it is required for hydrolysis of cholesteryl esters and triglycerides from low density lipoproteins (LDL) to generate fatty acids and cholesterol (2). LIPA deficiency from over 40 reported loss-of-function mutations leads to accumulation of cholesterol and triglyceride in the lysosome with resulting dysfunctional cholesterol homeostasis (1, 3). Lysosomal acid deficiency (LAL-D) is an autosomal recessive lysosomal storage disease with two phenotypes including early-onset Wolman disease (WD) and later-onset cholesteryl ester storage disease (CESD) (3, 4). Supplementation of LIPA through enzyme replacement therapy has been shown to be effective and is the standard therapy for LAL-deficiency although additional treatments are being explored (3, 4-6). Due to its central role in lipid regulation, altered function and variants of LIPA have also been implicated in development of atherosclerotic disease and coronary artery disease (1, 3, 7, 8). LIPA has additionally been reported as a therapeutic target for cancer and solid tumors through its role in induction of ER stress (9), its association with specific binding partner of interest (10), and its ability to modulate lipid metabolism in cancer cells (11).