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P4680

Sigma-Aldrich

Anti-Protein C antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

western blot: 1:500

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PROC(5624)

General description

Protein C (PROC) or activated protein C is a serine protease. It is expressed in the lungs. The gene encoding this protein is localized on human chromosome 2q14.
Protein C is synthesized by liver parenchymal cells as a single chain polypeptide, but in plasma, it consists mainly of a heavy chain (41 kDa) linked by a disulfide bond to a light chain (21 kDa). The plasma concentration of protein C is ~ 4 mg/mL with a half-life of about 15 hours.

Specificity

Specifically reacts with protein C in normal pooled human plasma and shows no reaction with protein C-depleted plasma.

Immunogen

Protein C from human plasma.

Application

Anti-Protein C antibody produced in rabbit has been used to study the effects of zirconia-based stationary phase on its activity.
Anti-Protein C may be used for the immunochemical determination of protein C levels in normal and pathogenic human plasma. Determination of protein C levels can be used in the study of regulation of blood coagulation and fibrinolysis.

Biochem/physiol Actions

Protein C (PROC) functions as a cytoprotective anticoagulant and has anti-inflammatory effects. PROC inactivates factors Va and VIIIa. The protein stabilizes the endothelial barrier and thereby reduces vascular permeability. It also modulates gene expression.
Protein C is a vitamin K-dependent plasma zymogen which plays an essential role in the regulation of blood coagulation. Activated protein C also enhances fibrinolysis by forming a complex with plasminogen activator inhibitor, thus allowing enhanced activity of plasminogen activator. Hereditary and acquired protein C deficiency states have been recognized to be associated with thrombosis. Homozygous severe protein C deficiency manifests in the new born by massive thrombosis and purpura fulminans. Heterozygotes for this entity usually do not manifest thrombosis.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

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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Mechanism of protein C-dependent clot lysis: role of plasminogen activator inhibitor
Sakata Y, et al.
Blood, 68(6), 1218-1223 (1986)
Activated protein C inhibits neutrophil extracellular trap formation in vitro and activation in vivo.
Healy LD
The Journal of Biological Chemistry, 292(21), 8616-8629 (2017)
The protein C pathway in tissue inflammation and injury: pathogenic role and therapeutic implications
Danese S, et al.
Blood, 115(6), 1121-1130 (2010)
Activation-Resistant Homozygous Protein C R229W Mutation Causing Familial Perinatal Intracranial Hemorrhage and Delayed Onset of Thrombosis
Abdulrahman Alsultan
Thrombosis Research, 143, 17-21 (2016)
Ruilong Zhao et al.
Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 32(1), 90-103 (2023-12-29)
Various preclinical and clinical studies have demonstrated the robust wound healing capacity of the natural anticoagulant activated protein C (APC). A bioengineered APC variant designated 3K3A-APC retains APC's cytoprotective cell signalling actions with <10% anticoagulant activity. This study was aimed

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