Mouse Anti-F9 Recombinant Antibody (CBXF-0202) (V2LY-0825-LY1164)

Name: Mouse Anti-F9 Recombinant Antibody (CBXF-0202)
SKU: V2LY-0825-LY1164
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-0202

Application

WB, IP

Immunogen

Purified human factor IX.

Host Species

Mouse

Specificity

Human

Antibody Isotype

IgG1

Clonality

Monoclonal Antibody

Application Notes

Application	Note
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)

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

Format

Liquid

Buffer

PBS, gelatin

Preservative

Sodium azide

Concentration

0.1 mg/ml

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.

More Infomation

Target

Full Name

Coagulation Factor IX

Entrez Gene ID

2158

UniProt ID

P00740

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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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

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Isotype control

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

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