Recombinant Human Protein S/PROS1, CF

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When Recombinant Human Tyro3/Dtk Fc Chimera (Catalog # 859‑DK) is immobilized at 1 μg/mL, 100 μL/well, Recombinant Human Protein S/PROS1 (Catalog # 9489‑PS)binds with an ED50 of0.2-1.2 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Protein S/PROS1, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Tyro3/Dtk Fc Chimera (Catalog # 859-DK) is immobilized at 1 μg/mL, 100 μL/well, Recombinant Human Protein S/PROS1 binds with an ED50 of 0.2-1.2 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human Protein S/PROS1 protein
Ala42-Trp670, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ala42
Protein/Peptide Type
Recombinant Enzymes
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
71 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
66-93 kDa, reducing conditions
Publications
Read Publications using
9489-PS in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES, NaCl and CaCl2.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 1 mg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Protein S/PROS1, CF

  • EC 3.4.21
  • PROS
  • PROS1
  • protein S (alpha)
  • Protein S
  • protein Sa
  • PS21
  • PS22
  • PS23
  • PS24
  • PS25
  • PSA
  • vitamin K-dependent plasma protein S
  • vitamin K-dependent protein S

Background

Anticoagulant Protein S (PROS1) is a 71 kDa plasma vitamin K-dependent glycoprotein characterized by the presence of the post-translational modification of specific glutamic acid residues to gamma-carboxyglutamic acid (Gla) in the N-terminal region. In addition to the N-terminal Gla domain, mature PROS1 contains a thrombin‑sensitive thumb loop, four tandem EGF-like domains and a C-terminal sex hormone-binding globulin (SHBG) domain composed of two Laminin G (LG) domains (1). Human PROS1 shares 80% amino acid sequence identity with mouse PROS1. Hundreds of mutations have been reported throughout all the domains of the protein, typically resulting in PROS1 deficiency and an increase in the risk of thrombophilia (2, 3). PROS1 is expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response (4-9). PROS1 exists in plasma both in complex with C4b-binding protein (C4BP) (60%) and in a free form (40%). Both forms of PROS1 have anti-coagulant activity either directly through inhibition of Factor X systems and prothrombinase while in complex with C4BP (5, 10) or in its well-established role as a cofactor of activated protein C (APC) inactivation of procoagulants FVa and FVIIIa (4). The free form of PROS1 is also a ligand for a subfamily of receptor tyrosine kinases known as TAMs, which is composed of TYRO3, AXL, and MERTK (11). PROS1 binds these tyrosine kinase receptors through its LG domains to activate downstream signaling pathways involved in tumor development and progression (7, 8, 11, 12).
  1. Dahlback, B. et al. (1986) Proc. Natl. Acad. Sci. 83:4199.
  2. Garcia de Frutos, P. et al. (2007) J. Thromb. Haemost. 98:543.
  3. Heeb, M. J. (2008) Expert Rev. Hematol. 1:9.
  4. Walker, F.J. (1984 Sem. Thromb. Hemosta. 10:131.
  5. Heeb, M. J. et al. (2004) J. Thromb. Haemost. 2:1766.
  6. Che Mat, M. F. (2016) Int. J. Oncol. 49:2359.
  7. Abboud-Jarrous, G. et al. (2017) Oncotarget. 8:13986.
  8. Qin, J. et al. (2016) Sci. Rep. 6:26662.
  9. Davra, V. et al. (2016) Cancers (Basel). 8:E107.
  10. Hackeng, T. M. et al. (1994) J. Biol. Chem. 269:21051.
  11. Tsou, W.I. et al. (2014) J. Biol. Chem. 289:25750.
  12. Linger, R.M.A. et al. (2008) Adv. Cancer Res. 100:35.

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