FGG/Fibrinogen gamma chain Protein, Mouse (P.pastoris)

FGG (fibrinogen gamma chain) proteins cooperate with FGA and FGB to form an insoluble fibrin matrix that is critical for hemostasis and wound repair. Although FGG is not required for thrombosis, it stabilizes lesions and guides cell migration during epithelialization. FGG/Fibrinogen gamma chain Protein, Mouse (P.pastoris, Tag Free) is the recombinant mouse-derived FGG/Fibrinogen gamma chain, expressed by P. pastoris , with tag Free labeled tag.

The FGG (Fibrinogen gamma chain) protein collaborates with fibrinogen alpha (FGA) and fibrinogen beta (FGB) to polymerize and form an insoluble fibrin matrix, a crucial element in hemostasis and blood clot formation. Additionally, FGG functions in the early stages of wound repair by stabilizing lesions and guiding cell migration during re-epithelialization. Despite initial beliefs suggesting its essential role in platelet aggregation, subsequent in vivo studies revealed that FGG is not absolutely required for thrombus formation. FGG also plays a role in enhancing the expression of SELP in activated platelets through an ITGB3-dependent pathway. Moreover, maternal fibrinogen is vital for successful pregnancy, and fibrin deposition is associated with infection, providing protection against IFNG-mediated hemorrhage. FGG may further contribute to the immune response through both innate and T-cell mediated pathways. Structurally, FGG forms a heterohexamer through disulfide linkage, consisting of two sets of three non-identical chains (alpha, beta, and gamma), arranged in a head-to-head conformation with the N-termini in a small central domain.

Mouse

P. pastoris

Tag Free

Q8VCM7 (V168-V436)

99571

30.5 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.