

| Numéro de catalogue | HC713012 |
|---|---|
| Description |
Recombinant Human LIPA Protein, N-His (HC713012) expressed in E. coli, spanning Asp30-Gln399. Purity: >90% by SDS-PAGE.
Highlights
|
| Système d'expression | E. coli |
| Numéro d'accès | P38571 |
| Longueur de protéine | Asp30-Gln399 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Espèces | Homo sapiens (Human) |
| Nature | Recombinant |
| Niveau d'endotoxines | Please contact with the lab for this information. |
| Pureté | >90% as determined by SDS-PAGE. |
| Masse moléculaire prédite | 44.58 kDa |
| Forme | Lyophilized |
| Tampon de stockage | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Expédition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stabilité et stockage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Noms alternatifs | Acid cholesteryl ester hydrolase, Cholesteryl esterase, Diacylglycerol lipase, EC:3.1.1.13, LAL, LIPA, Lipase A, Lysosomal acid lipase/cholesteryl ester hydrolase, Sterol esterase, Triacylglycerol ester hydrolase, Triacylglycerol lipase |
| Contexte | Lysosomal acid lipase/cholesteryl ester hydrolase is a ~45 kDa protein. Catalyzes the deacylation of cholesteryl ester core lipids of endocytosed low density lipoproteins to generate free fatty acids and cholesterol. Hydrolyzes triglycerides (1,2,3-triacylglycerol) and diglycerides (such as 1,2-diacylglycerol and 1,3-diacylglycerol) with preference for the acyl moieties at the sn-1 or sn-3 positions. 1. Zschenker, O. et al. (2004) Journal of biochemistry 136, 65-72. PMID: 15269241 2. Anderson, RA. et al. (1991) The Journal of biological chemistry 266, 22479-84. PMID: 1718995 3. Warner, TG. et al. (1981) The Journal of biological chemistry 256, 2952-7. PMID: 7204383 4. Ameis, D. et al. (1994) European journal of biochemistry 219, 905-14. PMID: 8112342 5. Ries, S. et al. (1998) Human mutation 12, 44-51. PMID: 9633819 |
| Note | For research use only |
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