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P2200

Sigma-Aldrich

Protein C from human plasma

Activated, lyophilized powder, ≥90% (SDS-PAGE)

Synonym(s):

Activated Protein C

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

human plasma

Quality Level

Assay

≥90% (SDS-PAGE)

form

lyophilized powder

mol wt

heavy chain 41 kDa
light chain 21 kDa

technique(s)

inhibition assay: suitable

solubility

H2O: 1 mg/mL

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... PROC(5624)

General description

Protein C from human plasma is encoded by the gene PROC. In human chromosome, the gene is localised on chromosome 2q14. Activated protein C (APC) cleaves protease activated receptor 1 (PAR1) resulting in cytoprotective and anti-inflammatory effects. Clinical trials with APC implicates its use in treating severe early onset preeclampsia in pregnant women and prolongs pregnancy and helps in perinatal outcomes.

Application

Protein C from human plasma has been used for pre-treatment of endothelial cells prior to antibody-inhibition assay. It has also been used in activated protein C (APC) assay to determine its inhibitory effect on copper.

Biochem/physiol Actions

In addition, activated protein C has been shown to inhibit TNF-α induced expression of the inflammatory proteins VCAM, ICAM-I, and Ilk-8 in endothelial cells.
Protein C is a plasma, vitamin κ-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating Factors Va and VIIIa.
Protein C is a plasma, vitamin κ-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating Factors Va and VIIIa. The Protein C anticoagulant pathway is triggered when thrombin binds to the endothelial cell proteoglycan, thrombomodulin. This complex, which cannot clot blood, is a potent activator of the protein C zymogen. Activation involves the release of a dodecapeptide from the N-terminal domain of the heavy chain. The activated Protein C (APC) then binds to protein S on cell surfaces and inactivates the coagulation factors Va and VIIIa by proteolysis. APC has also been shown to bind to receptors on the endothelium of large blood vessels.

Physical form

Lyophilized powder from 20 mM Tris-HCl, pH 7.4, containing 0.1 M NaCl

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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K A Hill et al.
The Journal of biological chemistry, 262(1), 140-146 (1987-01-05)
A pre-steady state kinetic analysis of the stimulation by monovalent cations of the activity of bovine activated protein C (APC) and a proteolytic fragment of APC, des-1-41-light chain activated protein C (GDAPC), toward the substrate, 4-methylumbelliferyl p-guanidinobenzoate, has been undertaken.
Rahul Kumar et al.
The Korean journal of pain, 32(3), 168-177 (2019-07-02)
Brennan's rodent paw incision model has been extensively used for understanding mechanisms underlying postoperative pain in humans. However, alterations of physiological parameters like blood pressure and heart rate, or even feeding and drinking patterns after the incision have not been
Severe malaria is associated with parasite binding to endothelial protein C receptor
Turner L, et al.
Nature, 498(7455), 502-502 (2013)
David Stacey et al.
Nature communications, 13(1), 1222-1222 (2022-03-11)
Many individual genetic risk loci have been associated with multiple common human diseases. However, the molecular basis of this pleiotropy often remains unclear. We present an integrative approach to reveal the molecular mechanism underlying the PROCR locus, associated with lower
K A Hill et al.
The Journal of biological chemistry, 261(32), 14991-14996 (1986-11-15)
The kinetic properties of the activation by monovalent cations of the amidolytic activity of bovine des-1-41 light chain activated protein C have been examined. With the cations Cs+, K+, Li+, and Tl+, a single cation site, or class of sites

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