Mouse Anti-F7 Recombinant Antibody (CBXF-2769) (CBMAB-F3486-CQ)

Name: Mouse Anti-F7 Recombinant Antibody (CBXF-2769)
SKU: CBMAB-F3486-CQ
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBXF-2769

Application

ELISA

Immunogen

Human F7.

Host Species

Mouse

Specificity

Human

Antibody Isotype

IgG1, κ

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
ELISA	1:100-1:1,000

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

Format

Liquid

Buffer

PBS, gelatin

Preservative

Sodium azide

Concentration

Batch dependent

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Epitope

AA 39-444

More Infomation

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
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For research use only. Not intended for any clinical use.

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