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Mouse ANGPTL3 Recombinant Protein (C-His) (MV176011)

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Overview
Catalog No.MV176011
Description
Recombinant Mouse ANGPTL3 Protein, C-His (MV176011) expressed in Mammalian Cells, spanning Ser17-Thr206. Purity: >90% by SDS-PAGE.
Highlights
  • His-Tagged — N-terminal 6×His tag for IMAC purification.
  • Mammalian Expression — Proper folding and native glycosylation.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemMammalian cells
AccessionQ9R182
Protein lengthSer17-Thr206
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesMus musculus (Mouse)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 24.81 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 NamesANG-5, ANGPT5, ANGPTL3, ANGPTL3(17-221), ANGPTL3(17-224), Angiopoietin-5, Angiopoietin-like protein 3, Angiopoietin-related protein 3
Background

Angiopoietin-related protein 3 is a ~52 kDa protein. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity; the function seems to be specific for the feeding conditions. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids; the cleaved N-terminal domain is more efficient than the uncleaved proprotein.

1. Koishi, R. et al. (2002) Nature genetics 30, 151-7. PMID: 11788823
2. Ando, Y. et al. (2003) Journal of lipid research 44, 1216-23. PMID: 12671033
3. Wang, Y. et al. (2015) Proceedings of the National Academy of Sciences of the United States of America 112, 11630-5. PMID: 26305978
4. Ono, M. et al. (2003) The Journal of biological chemistry 278, 41804-9. PMID: 12909640
5. Köster, A. et al. (2005) Endocrinology 146, 4943-50. PMID: 16081640
6. Liu, J. et al. (2010) The Journal of biological chemistry 285, 27561-70. PMID: 20581395
7. Jin, W. et al. (2007) Cell metabolism 6, 129-36. PMID: 17681148
8. Wang, Y. et al. (2015) Journal of lipid research 56, 1296-307. PMID: 25954050
9. Kim, HK. et al. (2015) Diabetes 64, 1142-53. PMID: 25338813
Note For research use only
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
Mass
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Volume
Molecular Weight *
g/mol
Formula
C₁ × V₁ = C₂ × V₂
Enter any 3 of the 4 values to solve for the unknown.
Stock Solution
C₁ (Stock Conc.)
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V₁ (Stock Vol.)
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Working Solution
C₂ (Working Conc.)
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V₂ (Working Vol.)
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