Cynomolgus Recombinant F9 protein, His Tag (V2LY-0526-LY1506)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Cynomolgus
Tag
His Tag
Protein Construction
This product is Cynomolgus Recombinant F9 protein, His Tag consist of Amino Acid: 1-461 and predicts a molecular mass of 50.17 kDa.
Molecule Mass
50.17 kDa
Verified
HPLC
Sequence
Amino Acid: 1-461
Species
Cynomolgus

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 PBS
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 IX
Research Area
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.
Biological Process
Blood coagulation Source: UniProtKB
Proteolysis Source: UniProtKB
Zymogen activation Source: UniProtKB
Cellular Location
Secreted
Involvement in disease
Hemophilia B (HEMB):
An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide (PubMed:12588353, PubMed:2738071, PubMed:3009023, PubMed:8295821, PubMed:9169594, PubMed:9600455, PubMed:25251685). Mutation in position 93 (Alabama) probably fails to bind to cell membranes (PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya or Hilo) prevent cleavage of the activation peptide (PubMed:6603618, PubMed:8076946, PubMed:12588353, PubMed:2162822, PubMed:25251685, PubMed:2713493).
Thrombophilia, X-linked, due to factor IX defect (THPH8):
A hemostatic disorder characterized by a tendency to thrombosis.
Warfarin sensitivity, X-linked (WARFS):
A condition characterized by sensitivity to warfarin, a drugs used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. Warfarin sensitive individuals develop bleeding complications when they are given warfarin within the therapeutic ranges.
PTM
Activated by factor XIa, which excises the activation peptide (PubMed:9169594, PubMed:1730085). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729).
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Carpintero-Fernández, P., Borghesan, M., Eleftheriadou, O., Pan-Castillo, B., Fafián-Labora, J. A., Mitchell, T. P., ... & O’Loghlen, A. (2022). Genome wide CRISPR/Cas9 screen identifies the coagulation factor IX (F9) as a regulator of senescence. Cell death & disease, 13(2), 1-13.

Branchini, A., Morfini, M., Lunghi, B., Belvini, D., Radossi, P., Bury, L., ... & Svahn, J. (2022). F9 missense mutations impairing factor IX activation are associated with pleiotropic plasma phenotypes. Journal of Thrombosis and Haemostasis, 20(1), 69-81.

Kihlberg, K., Baghaei, F., Bruzelius, M., Funding, E., Holme, P. A., Lassila, R., ... & Astermark, J. (2022). Factor IX antibodies and tolerance in hemophilia B in the Nordic countries–The impact of F9 variants and complications. Thrombosis Research, 217, 22-32.

Yin, R., & Liu, C. (2022). Human coagulation factor IX: a systematic review of its characteristics. Blood Coagulation & Fibrinolysis, 33(1), 1-7.

Carpintero-Fernández, P., Borghesan, M., Eleftheriadou, O., Fafián-Labora, J. A., Mitchell, T. P., Nightingale, T. D., ... & O’Loghlen, A. (2021). The coagulation factor IX (F9) loss of function prevents the cell cycle arrest induced by CDK4/6 inhibitors treatment. bioRxiv.

Iyer, N., Al Qaryoute, A., Kacham, M., & Jagadeeswaran, P. (2021). Identification of zebrafish ortholog for human coagulation factor IX and its age‐dependent expression. Journal of Thrombosis and Haemostasis, 19(9), 2137-2150.

Sidonio, R. F., & Malec, L. (2021). Hemophilia B (Factor IX Deficiency). Hematology/Oncology Clinics, 35(6), 1143-1155.

Mohammed, B. M., Cheng, Q., Matafonov, A., Monroe, D. M., Meijers, J. C., & Gailani, D. (2018). Factor XI promotes hemostasis in factor IX‐deficient mice. Journal of Thrombosis and Haemostasis, 16(10), 2044-2049.

Ferrarese, M., Testa, M. F., Balestra, D., Bernardi, F., Pinotti, M., & Branchini, A. (2018). Secretion of wild‐type factor IX upon readthrough over F9 pre‐peptide nonsense mutations causing hemophilia B. Human Mutation, 39(5), 702-708.

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

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