Analytical Data
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Gene name
FGL2
- Application
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Alternative Names
FGL2；Fibroleukin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14314
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Expression Region
24-439aa
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AA Sequence
NNETEEIKDERAKDVCPVRLESRGKCEEAGECPYQVSLPPLTIQLPKQFSRIEEVFKEVQNLKEIVNSLKKSCQDCKLQADDNGDPGRNGLLLPSTGAPGEVGDNRVRELESEVNKLSSELKNAKEEINVLHGRLEKLNLVNMNNIENYVDSKVANLTFVVNSLDGKCSKCPSQEQIQSRPVQHLIYKDCSDYYAIGKRSSETYRVTPDPKNSSFEVYCDMETMGGGWTVLQARLDGSTNFTRTWQDYKAGFGNLRREFWLGNDKIHLLTKSKEMILRIDLEDFNGVELYALYDQFYVANEFLKYRLHVGNYNGTAGDALRFNKHYNHDLKFFTTPDKDNDRYPSGNCGLYYSSGWWFDACLSANLNGKYYHQKYRGVRNGIFWGTWPGVSEAHPGGYKSSFKEAKMMIRPKHFKP
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Molecular Weight
49.6kDa
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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
Related Products
Protein Description
FGL2 (Fibrinogen-like protein 2) is a member of the fibrinogen family, primarily produced in the liver, and plays significant roles in various biological processes, including immune regulation, inflammation, and hemostasis. Research on FGL2 has gained traction due to its dual function; it acts as an immune modulator, influencing T cell responses and promoting immune tolerance, particularly in the context of infections and autoimmune diseases. Moreover, FGL2 has been implicated in tumor biology, where it may contribute to tumor progression and metastasis by modulating the tumor microenvironment and facilitating immune evasion. The complexity of its role in both immunity and cancer makes FGL2 a compelling target for therapeutic interventions. Recombinant FGL2 proteins have been developed to study its functional mechanisms and to evaluate its potential as a biomarker for disease progression or as a therapeutic agent. Understanding the structure-function relationship of FGL2 through recombinant protein studies can provide insights into its biological activities and therapeutic potential, paving the way for innovative strategies in treating conditions associated with its dysregulation.
