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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 Kits (42) and Fibrinogen alpha Chain Proteins (16) and many more products for this protein.
Showing 10 out of 111 products:
Human Polyclonal FGA Primary Antibody for WB - ABIN2776978
Jood, Danielson, Ladenvall, Blomstrand, Jern: Fibrinogen gene variation and ischemic stroke. in Journal of thrombosis and haemostasis : JTH 2008
Show all 2 references for ABIN2776978
Human Polyclonal FGA Primary Antibody for IF, IHC (p) - ABIN390830
Thomas, Wheeless, Stack, Johnson: Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption. in Biochemistry 1998
Human Polyclonal FGA Primary Antibody for IHC, WB - ABIN630126
Matsumoto, Matsuura, Aoki, Maehashi, Iwamoto, Ohkawa, Yoshida, Yanaga, Takada: An efficient system for secretory production of fibrinogen using a hepatocellular carcinoma cell line. in Hepatology research : the official journal of the Japan Society of Hepatology 2014
Cow (Bovine) Polyclonal FGA Primary Antibody for IHC, WB - ABIN2776977
Smolarczyk, Boncela, Szymanski, Gils, Cierniewski: Fibrinogen contains cryptic PAI-1 binding sites that are exposed on binding to solid surfaces or limited proteolysis. in Arteriosclerosis, thrombosis, and vascular biology 2005
To novel fibrinogen mutations have been identified (Aa17GlyalphaCys and Aa381SeralphaPhe) that cosegregate with dysfibrinogenemia in seven family members of a Chinese pedigree.
The study reports two novel mutations detected in the FGA and FGB (show FGB Antibodies) genes in two patients with inherited hypofibrinogenemia.
Nutrient overload-induced up-regulation of all three fibrinogen component subunits of the coagulation cascade provides a possible mechanism to explain the excess cardiovascular disease mortality observed in non-alcoholic fatty liver disease patients.
An analysis of the results obtained in this study and a critical review of previously published data indicate that gene polymorphisms in FGA and FGB (show FGB Antibodies) are not related to ischemic stroke in children
Results support the idea that fibrinogen alphaC regions are involved in the thickening of fibrin fibers.
The study identified a 5.9 kDa C-terminal fragment of the fibrinogen alpha chain as an early serum biomarker of fibrogenic processes in patients with liver disease.
The Aalpha-Val360 related cross-sectionally to physiologic, radiologic, and symptomatic markers of disease severity of PiZZ alpha1-antitrypsin deficiency.
Case Report: hepatocytes homozygous for a large FGA deletion can be genetically modified to restore Aalpha-chain protein expression and secrete a functional fibrinogen hexamer.
High plasma D-dimer, fibrinogen, and platelet levels are associated with epithelial ovarian cancer independently of venous thromboembolism.
Elevated pre-operative plasma fibrinogen level is associated with aggressive soft-tissue sarcoma.
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 Antibodies).
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