Analytical Data
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Gene name
FGG/Fibrinogen gamma chain
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简介
FGG/fibrinogen gamma chain proteins polymerize together with FGA and FGB to form the fibrin matrix, which is essential for blood clot formation. In addition to coagulation, it aids in early wound repair, stabilizes lesions, and guides cell migration. FGG/Fibrinogen gamma chain Protein, Human (P.pastoris) is the recombinant human-derived FGG/Fibrinogen gamma chain protein, expressed by P. pastoris , with tag free.
- Application
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Alternative Names
Fibrinogen gamma chain; FGG; PRO2061
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Species
Human
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Source
P. pastoris
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02679-1
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Expression Region
V169-L453
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Protein Length
Partial
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Molecular Weight
32.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Fibrinogen gamma chain (FGG) is a crucial component of the fibrinogen protein that plays a significant role in blood coagulation and wound healing. Understanding the structure and function of FGG is vital, as its dysregulation can lead to various hemorrhagic and thrombotic disorders. Recent advancements in recombinant protein technology have made it feasible to produce FGG in vitro, allowing researchers to investigate its functional properties and interactions within the coagulation cascade. The recombinant FGG can be utilized to explore its role in fibrin formation and stability, assess its involvement in fibrinolysis, and evaluate its impact on platelet function and wound healing processes. Moreover, studying FGG through recombinant techniques offers the potential to develop novel therapeutic applications, such as targeted treatments for coagulopathies or the development of advanced biomaterials that may enhance tissue repair. The research into FGG not only furthers our understanding of the coagulation system but also paves the way for innovative clinical solutions in managing blood-related disorders.
