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Mouse Anti-F7 Recombinant Antibody (CBXF-3455) (CBMAB-F1769-CQ)

This product is a mouse antibody that recognizes F7. The antibody CBXF-3455 can be used for immunoassay techniques such as: ELISA, RIA, WB.
See all F7 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-3455
Antibody Isotype
IgG1
Application
ELISA, RIA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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
Concentration
5 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
Coagulation Factor VII
Introduction
This gene encodes coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. This factor circulates in the blood in a zymogen form, and is converted to an active form by either factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of the factor VII, a heavy chain containing a catalytic domain and a light chain containing 2 EGF-like domains are generated, and two chains are held together by a disulfide bond. In the presence of factor III and calcium ions, the activated factor then further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Defects in this gene can cause coagulopathy. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing to generate mature polypeptides.
Entrez Gene ID
2155
UniProt ID
P08709
Alternative Names
Coagulation Factor VII; Eptacog Alfa; Coagulation Factor VII (Serum Prothrombin Conversion Accelerator); FVII Coagulation Protein; Proconvertin; EC 3.4.21.21;
Research Area
Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
Biological Process
Animal organ regeneration Source: Ensembl
Blood coagulation Source: BHF-UCL
Circadian rhythm Source: Ensembl
Positive regulation of blood coagulation Source: Ensembl
Positive regulation of cell migration Source: BHF-UCL
Positive regulation of leukocyte chemotaxis Source: BHF-UCL
Positive regulation of platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
Positive regulation of positive chemotaxis Source: BHF-UCL
Positive regulation of protein kinase B signaling Source: BHF-UCL
Protein processing Source: BHF-UCL
Response to 2,3,7,8-tetrachlorodibenzodioxine Source: Ensembl
Response to anticoagulant Source: Ensembl
Response to astaxanthin Source: Ensembl
Response to carbon dioxide Source: Ensembl
Response to cholesterol Source: Ensembl
Response to estradiol Source: Ensembl
Response to estrogen Source: Ensembl
Response to genistein Source: Ensembl
Response to growth hormone Source: Ensembl
Response to hypoxia Source: Ensembl
Response to Thyroid stimulating hormone Source: Ensembl
Response to thyrotropin-releasing hormone Source: Ensembl
Response to thyroxine Source: Ensembl
Response to vitamin K Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Factor VII deficiency (FA7D):
A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
PTM
The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
O- and N-glycosylated. N-glycosylation at Asn-205 oCcurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines.
Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.

Tang, H., Luan, X., Li, J., Jiang, G., Zhen, H., Li, H., ... & Zhou, J. (2022). Novel heterozygous F7 gene mutation (c. C1286T) associated with congenital factor VII deficiency: A case report and literature review. Journal of Clinical Laboratory Analysis, 36(5), e24349.

Ouardani, C., Elmahmoudi, H., ELborgi, W., Gharbi, M., Meriem, A., & Gouider, E. (2022). Clinical phenotype and F7 gene genotype in 40 Tunisian patients with congenital factor VII deficiency. Blood Coagulation & Fibrinolysis, 33(5), 280-284.

Mashayekhi, A., & Ghasemi, E. (2022). Coagulation Factor VII: Genetic, Molecular, and Clinical Characteristics. Trends in Medical Sciences, 2(1).

Osaki, K., Sogabe, Y., Seki, R., Nakamura, T., Morishige, S., Oku, E., ... & Okamura, T. (2022). Factor VII Deficiency Due to Compound Heterozygosity for the p. Leu13Pro Mutation and a Novel Mutation in the HNF4 Binding Region (− 58G> C) in the F7 Promoter. The Kurume Medical Journal, MS6723006.

Bernardi, F., & Mariani, G. (2021). Biochemical, molecular and clinical aspects of coagulation factor VII and its role in hemostasis and thrombosis. haematologica, 106(2), 351.

Zhang, X., Wang, S., Leng, S., Feng, Q., Zhang, Y., Xu, S., ... & Sheng, Z. (2021). Novel factor VII gene mutations in six families with hereditary coagulation factor VII deficiency. Journal of Clinical Laboratory Analysis, 35(9), e23905.

Giansily‐Blaizot, M., Rallapalli, P. M., Perkins, S. J., Kemball‐Cook, G., Hampshire, D. J., Gomez, K., ... & McVey, J. H. (2020). The EAHAD blood coagulation factor VII variant database. Human Mutation, 41(7), 1209-1219.

Shahbazi, S., & Mahdian, R. (2019). Factor VII gene defects: review of functional studies and their clinical implications. Iranian biomedical journal, 23(3), 165.

Pongjantarasatian, S., Kadegasem, P., Sasanakul, W., Sa-Ngiamsuntorn, K., Borwornpinyo, S., Sirachainan, N., ... & Hongeng, S. (2019). Coagulant activity of recombinant human factor VII produced by lentiviral human F7 gene transfer in immortalized hepatocyte-like cell line. Plos one, 14(8), e0220825.

Olson, N. C., Raffield, L. M., Lange, L. A., Lange, E. M., Longstreth Jr, W. T., Chauhan, G., ... & Tracy, R. P. (2018). Associations of activated coagulation factor VII and factor VII a‐antithrombin levels with genome‐wide polymorphisms and cardiovascular disease risk. Journal of thrombosis and haemostasis, 16(1), 19-30.

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

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