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Mouse Anti-FGB Recombinant Antibody (CBXF-0522) (CBMAB-F2314-CQ)

This product is a mouse antibody that recognizes FGB. The antibody CBXF-0522 can be used for immunoassay techniques such as: ELISA, IHC-P, WB.
See all FGB antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-0522
Antibody Isotype
IgG1, κ
Application
ELISA, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, pH 7.2
Preservative
15 mM sodium azide
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Fibrinogen Beta Chain
Introduction
The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
2244
UniProt ID
P02675
Alternative Names
Fibrinogen Beta Chain; Fibrinogen, B Beta Polypeptide; Epididymis Secretory Sperm Binding Protein Li 78p; Beta-Fibrinogen; HEL-S-78p;
Research Area
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin 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. 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
Adaptive immune response Source: UniProtKB-KW
Blood coagulation, fibrin clot formation Source: UniProtKB
Cell adhesion Source: GO_Central
Cell-matrix adhesion Source: BHF-UCL
Cellular protein-containing complex assembly Source: BHF-UCL
Cellular response to interleukin-1 Source: Ensembl
Cellular response to leptin stimulus Source: Ensembl
Fibrinolysis Source: UniProtKB
Induction of bacterial agglutination Source: CACAO
Innate immune response Source: UniProtKB-KW
Negative regulation of endothelial cell apoptotic process Source: BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Plasminogen activation Source: UniProtKB
Platelet aggregation Source: BHF-UCL
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
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.

Ceznerová, E., Kaufmanová, J., Sovová, Ž., Štikarová, J., Loužil, J., Kotlín, R., & Suttnar, J. (2022). Structural and Functional Characterization of Four Novel Fibrinogen Mutations in FGB Causing Congenital Fibrinogen Disorder. International journal of molecular sciences, 23(2), 721.

Klajmon, A., Chmiel, J., Ząbczyk, M., Pociask, E., Wypasek, E., Malinowski, K. P., ... & Natorska, J. (2022). Fibrinogen β chain and FXIII polymorphisms affect fibrin clot properties in acute pulmonary embolism. European Journal of Clinical Investigation, 52(4), e13718.

Choe, H. M., Quan, B. H., Paek, H. J., Luo, Z. B., Gao, K., Han, S. Z., ... & Yin, X. J. (2022). Altered fibrinogen level and fibrin clot structure in myostatin homozygous mutant pig. Animal Genetics.

Bian, Z., Yamashita, T., Shi, X., Feng, T., Yu, H., Hu, X., ... & Abe, K. (2021). Accelerated accumulation of fibrinogen peptide chains with Aβ deposition in Alzheimer’s disease (AD) mice and human AD brains. Brain Research, 1767, 147569.

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.

Simurda, T., Vilar, R., Zolkova, J., Ceznerova, E., Kolkova, Z., Loderer, D., ... & Kubisz, P. (2020). A novel nonsense mutation in FGB (c. 1421G> A; p. Trp474Ter) in the beta chain of fibrinogen causing hypofibrinogenemia with bleeding phenotype. Biomedicines, 8(12), 605.

Rakmanotham, A., Ittiwut, R., Komwilaisak, P., Shotelersuk, V., Sosothikul, D., & Suphapeetiporn, K. (2020). A novel deletion in the fibrinogen beta chain (FGB) gene causing hypofibrinogenemia. Thrombosis Research, 186, 26-29.

Cai, R., Li, Y., Wang, W., Gao, X., Liu, M., Diao, Y., ... & Feng, Q. (2018). A novel fibrinogen variant in a Chinese pedigree with congenital dysfibrinogenemia caused by FGA P. Arg38Thr mutation: a case report. Medicine, 97(40).

Repetto, O., Maiero, S., Magris, R., Miolo, G., Cozzi, M. R., Steffan, A., ... & De Re, V. (2018). Quantitative proteomic approach targeted to fibrinogen β chain in tissue gastric carcinoma. International Journal of Molecular Sciences, 19(3), 759.

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

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