Factor X 250unit powder and solvent for solution for injection vials
Requires a prescription from a doctor or prescriber
Coagulation Factor X (Human), is a plasma-derived human blood coagulation factor is used by adults and children (aged 12 years and above) with hereditary Factor X deficiency.
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Coagadex 250unit powder and solvent for solution for injection vials
Therapeutically similar medicines
Similarity is based on WHO Anatomical Therapeutic Chemical (ATC) classification and on a factual NHS dm+d therapeutic-grouping code prefix. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
Guidelines from the National Institute for Health and Care Excellence
NICE clinical guidance(14)
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Source: National Institute for Health and Care Excellence (NICE). Contains public sector information licensed under the Open Government Licence v3.0.
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Codes for healthcare professionals and prescribing systems
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SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF code shown is the factual mapping value distributed by NHS Business Services Authority (NHSBSA) in the dm+d supplementary file under OGL v3.0; it is not affiliated with, nor licensed from, the publishers of the British National Formulary. ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Academic studies and reviews for this medicine's active substance
Showing all 30 studies.
Reviews & meta-analyses: 3 · 1970–2021
Showing all 30 studies, sorted by most relevant.
P. Greipp, R. Kyle, E. Bowie
American Journal of Hematology, 1981
- Adrenal Cortex Hormones
- Amyloidosis
- Blood Coagulation
E. Camerer, Wei Huang, S. Coughlin
Proceedings of the National Academy of Sciences of the United States of America, 2000
- Calcium
- Cell Line
- Cytoplasm
G. Dieijen, G. Tans, J. Rosing, et al.
The Journal of biological chemistry, 1981
- Calcium
- Cattle
- Enzyme Activation
The kinetic parameters of bovine factor X activation by bovine factor IXa have been determined in the absence and presence of Ca2+, thrombin-activated bovine factor VIII (VIIIa), and phospholipid (dioleoylphosphatidylcholine/dioleoylphosphatidylserine, 75/25; mol/mol). Factor IXa in the absence of Ca2+, factor VIIIa, and phospholipid is able to catalyze factor X activation. The Km for factor X is 299 microM which is well above its concentration in bovine plasma, about 0.2 microM. The Vmax of factor Xa formation is 0.0022 mol of Xa . min-1 . mol of IXa-1 under these conditions. Addition of Ca2+ has little effect on the kinetic constants of factor X activation by factor IXa. In the presence of 10 mM CaCl2 the Km for factor X is 181 microM, and the Vmax is 0.0105 mol of Xa . min-1 . mol of IXa-1. The presence of 10 microM phospholipid dramatically decreases the Km for factor X to 0.058 microM, and the Vmax becomes 0.0025 mol of Xa . min-1 . mol of IXa-1. The Vmax of factor Xa formation slightly increases when more phospholipid is present in our experiments, and there is a considerable increase of the Km for factor X at higher phospholipid concentrations. Therefore, the Km measured in the presence of phospholipid has to be regarded as an apparent Km. The possible explanations for this phenomenon are discussed. For the complete factor X-activating complex (i.e. factor IXa, factor VIIIa, Ca2+, and 10 microM phospholipid) the Km for factor X is 0.0063 microM, and the Vmax is raised 200,000-fold to 500 mol of Xa . min-1 . mol of IXa-1. In order to exert its stimulating effect on factor X activation factor VIII has to be activated with thrombin. Our results show that factor IXa is an enzyme which can activate factor X at a very low rate. The stimulating effect of phospholipid in factor X activation is mainly due to an effect on the Km for factor X, bringing it within the range of the plasma concentration. The stimulatory effect of factor VIIIa is explained by its 200,000-fold increase of the Vmax of factor Xa formation.
Abstract licence: CC BY
R. Scipio, M. Hermodson, S. G. Yates, et al.
Biochemistry, 1977
- Blood Proteins
- Factor IX
- Factor X
Fran Balkwill
Cytokine & Growth Factor Reviews, 2002
- Clinical Trials as Topic
- Disease Models, Animal
- Inflammation
C. Scotton, M. Krupiczojc, M. Königshoff, et al.
The Journal of clinical investigation, 2009
- Actins
- Base Sequence
- Bleomycin
J. Rosing, J. Rijn, E. Bevers, et al.
Blood, 1985
S. Gordon, B. Cross
The Journal of clinical investigation, 1981
- Cysteine Endopeptidases
- Neoplasm Proteins
- Blood Coagulation
Stuart G. Gordon, Stuart G. Gordon, John J. Franks, et al.
Thrombosis research, 1975
- Blood Coagulation
- Cattle
- Enzyme Precursors
S. Bajaj, S. Rapaport, C. Prodanos
Preparative biochemistry, 1981
- Chromatography, Affinity
- Electrophoresis, Polyacrylamide Gel
- Factor IX
Sources: aggregated from Europe PMC (EMBL-EBI), OpenAlex, Crossref, PubMed and other open scholarly databases. Retracted articles are excluded. Study information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
Not available
Mechanism
Factor X is an inactive zymogen that is synthesized in the liver, which can be a…
Food interactions
None known
Human targets
None mapped
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
[L41045]
Half-life
[L41045]
Volume of distribution
[L41045]
Clearance
[L41045]
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Coagulation Factor X is a vitamin K-dependent, liver-produced serine protease that serves as the first enzyme in the coagulation cascade to form fibrin. It is a two-chain glycoprotein with the molecular weight of approximately 59 kDa [A31472]. While Factor X normally circulates in the plasma as inactive molecules, the activation of Factor X is involved in both the intrinsic and extrinsic coagulation pathways. Inherited factor X deficiency is a rare autosomal recessive bleeding disorder that is estimated to occur in 1:1 000 000 individuals up to 1:500 carriers [A31471]. Administration of coagulation Factor X from healthy donor serves to restore and achieve effective hemostasis.
Coagulation Factor X (Human) solution is approved by the FDA for intravenous injection under the market name Coagadex which contains normally 100 IU/mL of coagulation Factor X derived from healthy donors who have passed viral screening tests [L41045].
[L41045]
Along with other blood coagulation factors, it is used to reverse acquired coagulation factor deficiency induced by Vitamin K antagonist (VKA, e.g., warfarin) therapy in adult patients with a need for an urgent surgery/invasive procedure.
[L12834][L50517]
Known interactions with other medications. Always consult a healthcare professional.
Showing 50 of 90 interactions
Factor Xa plays a critical initiation step of the coagulation pathway by cleaving and activating prothrombin to thrombin in complex with FVa, Ca2+ and phospholipids. This complex is also known as the prothrombinase complex. Thrombin then acts upon soluble fibrinogen and Factor XIII to generate a cross-linked fibrin clot [A19411][L41045].
How the body processes this drug — absorption, distribution, metabolism, and elimination
[L41045]
[L41045]
[L41045]
[L41045]
ATC B02BD13
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
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Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Coagulation factor X human
Matched from: Factor X
DrugBank citations
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Structured knowledge from the free knowledge base
Molecular structure
ATC classifications (Wikidata)
Linked open data from Wikidata (Q423701), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication. Molecular structure images from Wikimedia Commons.