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The protein encoded by FGA is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Additionally we are shipping Fibrinogen alpha Chain Antibodies (117) and Fibrinogen alpha Chain Kits (45) and many more products for this protein.
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The molecular characterization of two novel afibrinogenemic mutations in the fibrinogen A alpha and fibrinogen B beta chain establishes the importance of the A alpha and B beta C-terminal region for normal fibrinogen assembly and secretion.
This meta-analysis results did not show significant associations between the polymorphisms in FGA and Ischemic stroke.
there was a relatively high frequency of pregnancy loss in the setting of the FGA Thr312Ala polymorphism.
Fibrinogen was significantly increased in pediatric patients with complicated appendicitis compared to patients with uncomplicated appendicitis or non-specific abdominal pain.
No association between three single nucleotide polymorphisms in the fibrinogen alpha gene and schizophrenia.
Fibrinogen Shanghai results in N-terminal truncation of Aalpha chain, which does not interfere with synthesis, assembly or secretion of fibrinogen, but compromises fibrin polymerization and clot (show TXNDC17 Proteins) formation.
We found a mutation that consists of a R458C substitution on the fibrinogen alpha chain gene confirmed in 13 new familial subjects that causes a rare subtype of dysfibrinogenemia characterized by venous thromboembolic events
Fibrinogen Nijmegen, a mutation at the same position, is causative for thrombosis, whereas fibrinogen Innsbruck appears to lead to a bleeding tendency, illustrating that even mutations at the same position can cause contrary symptoms.
Neutrophilic asthma patients and eosinophilic asthma patients had increased fibrinogen compared to controls.
To novel fibrinogen mutations have been identified (Aa17GlyalphaCys and Aa381SeralphaPhe) that cosegregate with dysfibrinogenemia in seven family members of a Chinese pedigree.
NMR solution structure of the bovine fibrinogen alphaC-domain fragment, including residues Aalpha374-538, reveals a type-I' beta-hairpin, restricted at the base by a C423-C453 disulfide linkage and a short turn preceding C423.
cellular fibrin uptake was diminished by elimination of CCR2-expressing cells.
Mice expressing a mutant form of fibrinogen cannot support fibrin formation exhibit compromised antimicrobial host defense.
Data indicate RU-505 as an effective inhibitor of the beta-amyloid (Abeta)-fibrinogen interaction.
Fbg deficiency was associated with enhanced hepatic expression of the transcription factor early growth response-1 (show EGR1 Proteins).
Data suggest the potential compensatory role of fibrinogen in restoring coagulation function in vivo after hemorrhagic shock.
The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus.
fibrinogen alpha chain
, fibrinogen alpha chain-like
, fibrinogen, A alpha polypeptide
, fibrinogen A-alpha chain
, fibrinogen, alpha polypeptide
, carboxy-terminal region
, fibrinogen A-alpha-chain
, fibrinogen alpha subunit
, fibrinogen alpha-E subunit
, pre-fibrinogen alpha subunit