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

R&D Systems | Catalog # 11633-LA

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Key Product Details

  • 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

Source

CHO

Accession Number

P38571.2

Applications

Enzyme Activity
View all LIPA Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human LIPA protein
Gly24-Gln399 with N-terminal HA (YPYDVPDYA) and 6-His tags

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Tyr

Predicted Molecular Mass

45 kDa

SDS-PAGE

55-67 kDa, under reducing conditions

Activity

Measured by its ability to cleave a fluorogenic substrate, 4-Methylumbelliferyl oleate (4-MUO).The specific activity is >7000 pmol/min/μg, as measured under the described conditions.

Scientific Data Images for Recombinant Human LIPA HA-tag His-tag Protein, CF

Recombinant Human LIPA HA-tag His-tag Enzyme Activity.

Recombinant Human LIPA HA-tag His-tag (Catalog # 11633-LA) is measured by its ability to cleave a fluorogenic peptide substrate, 4-Methylumbelliferyl oleate (4-MUO).

Recombinant Human LIPA HA-tag His-tag SDS-PAGE.

2 μg/lane of Recombinant Human LIPA HA-tag His-tag (Catalog # 11633-LA) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-67 kDa, under reducing conditions.

Formulation, Preparation, and Storage

11633-LA
Formulation Supplied as a 0.2 μm filtered solution in MES, NaCl and TCEP.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

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).

References

  1. Rajamohan, F. et al. (2020) J. Lipid Res. 61:1192.
  2. Anderson, R.A. and G.N. Sando (1991) J. Biol. Chem. 266:22479.
  3. Maciejko, J.J. (2017) Am. J. Cardiovasc. Drugs 17:217.
  4. Korbelius, M. et al. (2023) Trends Mol. Med. 29:425.
  5. Burton, B.K. et al. (2015) N. Engl. J. Med. 373:1010.
  6. Rader, D.J. (2015) N. Engl. J. Med. 373:1071.
  7. Wild, P.S. et al. (2011) Circ. Cardiovasc. Genet. 4:403.
  8. Li, F. and H. Zhang (2019) Arterioscler. Thromb. Vasc. Biol. 39:850.
  9. Liu, X. et al. (2022) Nat. Cancer 3:866.
  10. Collier, A.B. (2024) Cancers 16:500.
  11. Jin, Z. et al. (2024) Cancer Res. Commun. 4:2242.

Long Name

Lipase A

Alternate Names

CESD, Lipase A

Entrez Gene IDs

3988 (Human)

Gene Symbol

LIPA

UniProt

P38571.2

Additional LIPA Products

Product Documents for Recombinant Human LIPA HA-tag His-tag Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human LIPA HA-tag His-tag Protein, CF

For research use only

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Protocols

View specific protocols for Recombinant Human LIPA HA-tag His-tag Protein, CF (11633-LA):

Materials
  • Assay Buffer: 25 mM MES, 1% Triton X-100, pH 5.5  
  • Recombinant Human LIPA HA-tag His-tag (rhLIPA) (Catalog # 11633-LA)
  • Substrate: 4-Methylumbelliferyl oleate (4-MUO), 100 mM stock in DMSO
  • Black 96-well Plate
  • Plate Reader with Fluorescence Read Capability
  1. Dilute rhLIPA to 2 µg/mL in Assay Buffer.
  2. Dilute Substrate to 1.2 mM in Assay Buffer.
  3. Load into a plate 50 µL of 2 µg/mL rhLIPA and start the reaction by adding 50 µL of 1.2 mM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 1.2 mM Substrate. 
  4. Read at excitation and emission wavelengths of 365 nm and 445 nm (top read), respectively, in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

   

*Adjusted for Substrate Blank
**Derived using a fluorescent standard 4-Methylumbelliferone
Per Well:
  • rhLIPA: 0.1 µg
  • Substrate: 600 µM

























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