Human Recombinant FGG protein (V2LY-0526-LY4140)

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Basic Information

Expressed Host
Yeast
Protein Species
Human
Protein Construction
This product is Human Recombinant FGG protein consist of Amino Acid: 169-453 and predicts a molecular mass of 32.2 kDa.
Molecule Mass
32.2 kDa
Verified
HPLC
Sequence
Amino Acid: 169-453
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Fibrinogen Gamma Chain
Function
Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Biological Process
Blood coagulation, fibrin clot formation Source: UniProtKB
Cell-matrix adhesion Source: BHF-UCL
Cellular protein-containing complex assembly Source: BHF-UCL
Cellular response to interleukin-1 Source: Ensembl
Cellular response to interleukin-6 Source: Ensembl
Fibrinolysis Source: UniProtKB
Negative regulation of endothelial cell apoptotic process Source: BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Negative regulation of platelet aggregation Source: Ensembl
Plasminogen activation Source: UniProtKB
Platelet aggregation Source: BHF-UCL
Platelet maturation Source: Ensembl
Positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Positive regulation of exocytosis Source: BHF-UCL
Positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
Positive regulation of peptide hormone secretion Source: BHF-UCL
Positive regulation of protein secretion Source: BHF-UCL
Positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
Positive regulation of vasoconstriction Source: BHF-UCL
Protein polymerization Source: BHF-UCL
Protein secretion Source: UniProtKB
Response to calcium ion Source: BHF-UCL
Cellular Location
Secreted
Involvement in disease
Congenital afibrinogenemia (CAFBN):
The disease is caused by variants affecting the gene represented in this entry. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding. Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen.
Dysfibrinogenemia, congenital (DYSFIBRIN):
A disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia).
PTM
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.
Sulfation of C-terminal tyrosines increases affinity for thrombin.

Ceznerová, E., Kaufmanová, J., Stikarová, J., Pastva, O., Loužil, J., Chrastinová, L., ... & Dyr, J. E. (2022). Thrombosis-associated hypofibrinogenemia: novel abnormal fibrinogen variant FGG c. 8G> A with oxidative posttranslational modifications. Blood Coagulation & Fibrinolysis, 33(4), 228-237.

Liu, J. X., Wang, C. J., Dai, J. H., Zhang, M. X., Lyu, B., & Jiang, B. (2022). Fibrinogen gamma-chain mutation, p. Ile171His, leads to hereditary hypofibrinogenemia. Zhonghua nei ke za zhi, 61(2), 172-176.

Zhang, H., Li, C., Song, X., Cheng, L., Liu, Q., Zhang, N., ... & Li, F. (2021). Integrated analysis reveals lung fibrinogen gamma chain as a biomarker for chronic obstructive pulmonary disease. Annals of Translational Medicine, 9(24).

Zhang, W., Gao, Z., Zeng, G., Xie, H., Liu, J., Liu, N., & Wang, G. (2020). Clinical significance of urinary plasminogen and fibrinogen gamma chain as novel potential diagnostic markers for non-small-cell lung cancer. Clinica Chimica Acta, 502, 55-65.

Simurda, T., Brunclikova, M., Asselta, R., Caccia, S., Zolkova, J., Kolkova, Z., ... & Kubisz, P. (2020). Genetic variants in the FGB and FGG genes mapping in the beta and gamma nodules of the fibrinogen molecule in congenital quantitative fibrinogen disorders associated with a thrombotic phenotype. International Journal of Molecular Sciences, 21(13), 4616.

Liu, Y. L., Yan, Z. X., Xia, Y., Xie, X. Y., Zhou, K., Xu, L. L., ... & Bi, J. W. (2020). Ligustrazine reverts anthracycline chemotherapy resistance of human breast cancer by inhibiting JAK2/STAT3 signaling and decreasing fibrinogen gamma chain (FGG) expression. American journal of cancer research, 10(3), 939.

Paulsen, B., Skille, H., Smith, E. N., Hveem, K., Gabrielsen, M. E., Brækkan, S. K., ... & Hansen, J. B. (2020). Fibrinogen gamma gene rs2066865 and risk of cancer-related venous thromboembolism. haematologica, 105(7), 1963.

Wypasek, E., Klukowska, A., Zdziarska, J., Zawilska, K., Treliński, J., Iwaniec, T., ... & Undas, A. (2019). Genetic and clinical characterization of congenital fibrinogen disorders in Polish patients: Identification of three novel fibrinogen gamma chain mutations. Thrombosis Research, 182, 133-140.

Drizlionoka, K., Zariņš, J., Ozoliņa, A., Ņikitina-Zaķe, L., & Mamaja, B. (2019). Polymorphism rs2066865 in the Fibrinogen Gamma Chain (FGG) gene increases plasma fibrinogen concentration and is associated with an increased microvascular thrombosis rate. Medicina, 55(9), 563.

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For research use only. Not intended for any clinical use.

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