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Fibrinogen Alpha (FGa) Recombinant Protein | FGa recombinant protein
Recombinant Fibrinogen Alpha (FGa)
Avoid repeated freeze/thaw cycles.
Store at 2-8 degree C for one month.
Aliquot and store at -80 degree C for 12 months.
Stability Test:
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.
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NCBI and Uniprot Product Information
Accurate Molecular Mass: 14kDa as determined by SDS-PAGE reducing conditions.
NCBI Description
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. [provided by RefSeq, Jul 2008]
Uniprot Description
FGA: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Defects in FGA are a cause of congenital afibrinogenemia (CAFBN). 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. 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); 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. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: 4q28
Cellular Component: extracellular space; cell surface; fibrinogen complex; plasma membrane; extracellular region; cell cortex; vesicle; external side of plasma membrane
Molecular Function: protein binding, bridging; protein binding; cell adhesion molecule binding; structural molecule activity; receptor binding
Biological Process: protein polymerization; platelet activation; extracellular matrix organization and biogenesis; positive regulation of heterotypic cell-cell adhesion; cell-matrix adhesion; signal transduction; platelet degranulation; cellular protein complex assembly; positive regulation of protein secretion; positive regulation of vasoconstriction; innate immune response; response to calcium ion; blood coagulation; positive regulation of exocytosis
Disease: Amyloidosis, Familial Visceral; Afibrinogenemia, Congenital; Dysfibrinogenemia, Congenital
Research Articles on FGa
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Product Notes
The FGa fga (Catalog #AAA2012283) is a Recombinant Protein produced from E.coli and is intended for research purposes only. The product is available for immediate purchase. The Recombinant Fibrinogen Alpha (FGa) reacts with Homo sapiens (Human) and may cross-react with other species as described in the data sheet. AAA Biotech's Fibrinogen Alpha (FGa) can be used in a range of immunoassay formats including, but not limited to, Positive Control; Immunogen; SDS-PAGE; Western Blot (WB). (May be suitbable for use in other assays to be determined by the end user.). Researchers should empirically determine the suitability of the FGa fga for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: DNTYNRVSED LRSRIEVLKR KVIEKVQHIQ LLQKNVRAQL VDMKRLEVDI DIKIRSCRGS CSRALAREVD LKDYEDQQK QLEQVIAK DLLP. It is sometimes possible for the material contained within the vial of "Fibrinogen Alpha (FGa), Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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