When Recombinant Mouse Dtk Fc Chimera (Catalog # 759-DT) is immobilized at 1 μg/mL, 100 μL/well, Recombinant Mouse Protein S/PROS1 (Catalog # 9740‑PS) binds with an ED50 of 0.04-0.24 μg/mL.
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Tyro3/Dtk Fc Chimera (Catalog # 759-DT)
is immobilized at 1 μg/mL, 100 μL/well, Recombinant Mouse Protein S/PROS1
binds with an ED50 of 0.04-0.24 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Protein S/PROS1 protein Ala42-Arg669, with a C-terminal 10-His tag
>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
71-88 kDa, reducing conditions
Publications
Read Publications using 9740-PS in the following applications:
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 HEPES, NaCl, and CaCl2.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse 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). Mouse PROS1 shares 80% aa sequence identity with human PROS1. Hundreds of mutations in humans 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 anticoagulant 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 PROS-1 is
also a ligand for a subfamily of receptor tyrosine kinases known as TAMs, which
is composed of TYRO3, AXL, and MERTK (11). PROS-1 binds these tyrosine kinase
receptors through its LG domains to activate downstream signaling pathways
involved in tumor development and progression (7, 8, 11, 12).
Dahlback, B. et al. (1986) Proc. Natl. Acad. Sci. 83:4199.
Garcia de Frutos, P. et al. (2007) J. Thromb. Haemost. 98:543.
Heeb, M. J. (2008) Expert Rev. Hematol. 1:9.
Walker, F.J. (1984 Sem. Thromb. Hemosta. 10:131.
Heeb, M. J. et al. (2004) J. Thromb. Haemost. 2:1766.
Che Mat, M. F. (2016) Int. J. Oncol. 49:2359.
Abboud-Jarrous, G. et al. (2017) Oncotarget. 8:13986.
Qin, J. et al. (2016) Sci. Rep. 6:26662.
Davra, V. et al. (2016) Cancers (Basel). 8:E107.
Hackeng, T. M. et al. (1994) J. Biol. Chem. 269:21051.
Tsou, W.I. et al. (2014) J. Biol. Chem. 289:25750.
Linger, R.M.A. et al. (2008) Adv. Cancer Res. 100:35.
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