Native Human Fibrinogen protein (ab62394)
Key features and details
- Expression system: Native
- Purity: > 95% Size exclusion
- Suitable for: Functional Studies
Description
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Product name
Native Human Fibrinogen protein
See all Fibrinogen proteins and peptides -
Purity
> 95 % Size exclusion.
Purified by salt fractionation, size exclusion and ion exchange chromatography. -
Expression system
Native -
Protein length
Protein fragment -
Animal free
No -
Nature
Native -
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Species
Human
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Specifications
Our Abpromise guarantee covers the use of ab62394 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
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Form
Lyophilized -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituent: Tris buffered saline
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ReconstitutionAdd 1 ml of water for a final concentration of 200 micrograms/ml.
General Info
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Alternative names
- FGA
- FGB
- FGG
see all -
Function
Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. -
Tissue specificity
Plasma. -
Involvement in disease
Defects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. -
Sequence similarities
Contains 1 fibrinogen C-terminal domain. -
Domain
A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure. -
Post-translational
modificationsThe alpha chain is not glycosylated.
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.
Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Phosphorylation sites are present in the extracellular medium. -
Cellular localization
Secreted. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (1)
ab62394 has been referenced in 1 publication.
- Choi JW et al. Proteome Analysis of Human Natural Killer Cell Derived Extracellular Vesicles for Identification of Anticancer Effectors. Molecules 25:N/A (2020). PubMed: 33182448