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Human SGPL1 Recombinant Protein (N-His) (HF762022)

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Overview
Catalog No.HF762022
Description
Recombinant Human SGPL1 Protein, N-His (HF762022) expressed in E. coli, spanning Ser122-Tyr550. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionO95470
Protein lengthSer122-Tyr550
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 49.64 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

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.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage 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.
Alternate NamesEC:4.1.2.27, KIAA1252, S1PL, SGPL1, SP-lyase 1, SPL 1, Sphingosine-1-phosphate aldolase, Sphingosine-1-phosphate lyase 1, hSPL
Background

Sphingosine-1-phosphate lyase 1 is a ~63 kDa protein. Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP.

1. Van Veldhoven, PP. et al. (2000) Biochimica et biophysica acta 1487, 128-34. PMID: 11018465
2. Reiss, U. et al. (2004) The Journal of biological chemistry 279, 1281-90. PMID: 14570870
3. Weiler, S. et al. (2014) Journal of medicinal chemistry 57, 5074-84. PMID: 24809814
4. Lovric, S. et al. (2017) The Journal of clinical investigation 127, 912-928. PMID: 28165339
Note For research use only
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Formula
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