Mouse Recombinant F7 protein, His Tag (V2LY-0526-LY8292)

Name: Mouse Recombinant F7 protein, His Tag
SKU: V2LY-0526-LY8292
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

Expressed Host

CHO Stable Cells

Protein Species

Mouse

Tag

His Tag

Protein Construction

This product is Mouse Recombinant F7 protein, His Tag consist of Amino Acid: 1-446 and predicts a molecular mass of 47 kDa.

Molecule Mass

47 kDa

Sequence

Amino Acid: 1-446

Species

Mouse

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

Purity

>90% as determined by SDS-PAGE

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 Tirs, NaCl, Glycerol

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

Coagulation Factor VII

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
Other Protocols

Alternative Versions

Human Recombinant F7 protein, His Tag (CAT#: V2LY-0526-LY3992)

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

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