FGA; FGA protein; FGB; FGG; Fib2; Fibrin alpha chain ;Fibrinogen A alpha polypeptide; Fibrinogen A alpha polypeptide chain; Fibrinogen alpha chain; Fibrinogen B alpha polypeptide; Fibrinogen beta chain; Fibrinogen G alpha polypeptide; Fibrinogen gamma cha
Cat:
SL148G
Species Reactivity：
Human,(predicted: Mouse,Rat,)
Immunogen：
Fibrinogen from human plasma
Format：
Liquid
Storage instructions：
Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Concentration：
1mg/ml
Clonality：
Polyclonal
Isotype：
IgG
Applications：
WB=1:500-2000ELISA=1:5000-10000not yet tested in other applications.optimal dilutions/concentrations should be determined by the end user.
Host：
Goat
Product Overview：
Sample: Lane 1: Human Plasma Lane 2: Human Fibrinogen (from plasma)( SL148P) Primary: Anti-Fibrinogen (SL148G) at 1/1000 dilutionSecondary: IRDye800CW Donkey anti-Goat IgG at 1/20000 dilutionPredicted band size: 48 kDaObserved band size: 55,65,73 kDa
Fibrinogen is the main protein of blood coagulation system. It is a large protein and it consists of two identical subunits that contain three polypeptide chains: alpha, beta and gamma. All chains are connected with each other by a number of disulfide bonds. Fibrinopeptides A (1 to 16 amino acids) and B (1 to 17 amino acids) are released by thrombin from the N terminal parts of alpha and beta chains, respectively. In this way fibrinogen is converted into fibrin, which by means of polymerization forms a fibrin clot. Fibrinogen clotting underlies pathogenesis of MI, thromboembolism and thromboses of arteries and veins, since fibrin is the main substrate for thrombus formation. Fibrinogen activation is also involved in pathogenesis of inflammation, tumor growth and many other diseases.
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Subcellular Location: Secreted.
Tissue Specificity: Plasma.
Post-translational modifications: The 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.
Sample:
Lane 1: Human Plasma
Lane 2: Human Fibrinogen (from plasma)( SL148P)
Primary: Anti-Fibrinogen (SL148G) at 1/1000 dilution
Secondary: IRDye800CW Donkey anti-Goat IgG at 1/20000 dilution
Predicted band size: 48 kDa
Observed band size: 55,65,73 kDa
Product Feedback Wall
Specific References (1) | SL148G has been referenced in 1 publications.
[IF=4.882] Li Peichuang. et al. Preparation of phospholipid-based polycarbonate urethanes for potential applications of blood-contacting implants. Regen Biomater. 2020 Oct;7(5):491-504 ELISA ; Rabbit.
