P4680
Anti-Protein C antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
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)
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Mechanism of protein C-dependent clot lysis: role of plasminogen activator inhibitor
Blood, 68(6), 1218-1223 (1986)
Activated protein C inhibits neutrophil extracellular trap formation in vitro and activation in vivo.
The Journal of Biological Chemistry, 292(21), 8616-8629 (2017)
The protein C pathway in tissue inflammation and injury: pathogenic role and therapeutic implications
Blood, 115(6), 1121-1130 (2010)
Activation-Resistant Homozygous Protein C R229W Mutation Causing Familial Perinatal Intracranial Hemorrhage and Delayed Onset of Thrombosis
Thrombosis Research, 143, 17-21 (2016)
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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