F9 Recombinant Monoclonal Antibody

說明書

中文名稱：

F9重組抗體
貨號(hào)：

CSB-RA923075A0HU
規(guī)格：

￥1320
圖片：
Western Blot
Positive WB detected in: HepG2 whole cell lysate, A549 whole cell lysate, K562 whole cell lysate
All lanes: Factor IX antibody at 1:2000
Secondary
Goat polyclonal to rabbit IgG at 1/50000 dilution
Predicted band size: 52 kDa
Observed band size: 52 kDa
其他：

產(chǎn)品詳情
產(chǎn)品評(píng)價(jià)
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

產(chǎn)品描述：

F9 Recombinant Monoclonal Antibody（CSB-RA923075A0HU）是針對(duì)凝血因子IX（F9）研發(fā)的高特異性重組單克隆抗體。F9是凝血級(jí)聯(lián)反應(yīng)中關(guān)鍵的絲氨酸蛋白酶原，在肝臟合成后通過維生素K依賴性途徑激活，其功能缺陷與B型血友病密切相關(guān)。該抗體經(jīng)ELISA和蛋白質(zhì)印跡（WB）嚴(yán)格驗(yàn)證，在WB實(shí)驗(yàn)中可識(shí)別天然及重組F9蛋白，呈現(xiàn)單一清晰條帶，推薦使用稀釋度為1:500至1:5000，展現(xiàn)優(yōu)異的批次間穩(wěn)定性和檢測靈敏度。其重組抗體特性確保低交叉反應(yīng)性，適用于血漿樣本或細(xì)胞裂解液中F9蛋白的定量分析與功能研究。在科研領(lǐng)域，該產(chǎn)品可廣泛應(yīng)用于凝血機(jī)制研究、血友病疾病模型構(gòu)建，以及抗血栓或凝血因子替代療法的體外藥效評(píng)估，為探索F9在止血平衡、病理狀態(tài)下的調(diào)控作用提供可靠工具。
Uniprot No.：

P00740
基因名：

F9
別名：

Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain, Coagulation factor IXa heavy chain], F9
反應(yīng)種屬：

Human
免疫原：

A synthesized peptide derived from human Factor IX
免疫原種屬：

Homo sapiens (Human)
標(biāo)記方式：

Non-conjugated
克隆類型：

Monoclonal
抗體亞型：

Rabbit IgG
純化方式：

Affinity-chromatography
克隆號(hào)：

3G3
濃度：

It differs from different batches. Please contact us to confirm it.
保存緩沖液：

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.
產(chǎn)品提供形式：

Liquid
應(yīng)用范圍：

ELISA, WB

推薦稀釋比：

Application	Recommended Dilution
WB	1:500-1:5000

Protocols：

ELISA Protocol
Western Blotting (WB) Protocol
儲(chǔ)存條件：

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期：

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
用途：

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

功能：

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 Ca(2+) ions, phospholipids, and factor VIIIa.
基因功能參考文獻(xiàn)：
1. available to predict the inhibitory activity on FIXa. On the basis of pharmacophore modeling, molecular docking, and 3D-QSAR modeling screening, six molecules are PMID: 29724133
2. Report induced pluripotent stem cell model characterizing mutated F9 mRNA in hemophilia B. PMID: 28834196
3. genetic association studies in cohort of patients in Switzerland: Data suggest that F9 propeptide mutation-associated hypersensitivity to vitamin K antagonist anticoagulants is rare phenomenon; F9 propeptide mutation Ala37Thr confers high sensitivity to warfarin. PMID: 29450643
4. Higher FIX antigen levels are associated with incident coronary heart disease in blacks but not in whites; the association of FXI levels with ischemic stroke is slightly attenuated after adjusting for stroke risk factors. PMID: 28393470
5. a computational approach was conducted to select suitable location(s) for introducing new N-glycosylation sites into the human coagulation factor IX. PMID: 27356208
6. The pathogenic basis for one synonymous mutation (Val107Val) in the F9 gene associated with haemophilia B was determined. PMID: 28007939
7. caspase-3 inhibitors also suppressed the attenuation of cell adhesion and phosphorylation of p38 MAPK by EGF-F9. Our data indicated that EGF-F9 activated signals for apoptosis and induced de-adhesion in a caspase-3 dependent manner. PMID: 27129300
8. Specific factor IX mRNA and protein features that favor drug-induced readthrough over recurrent nonsense mutations have been reported. PMID: 28196793
9. Here we optimize the transient transfection of HEK293T/17 cells for the production of AAV human factor IX in a disposable fixed-bed bioreactor, the iCELLis((R)) Nano (PALL Corporation). PMID: 27229773
10. Thus, splicing and protein alterations contribute to define at the molecular level the disease-causing effect of a number of exonic mutations in coagulation FIX exon 5. In addition, our results have a significant impact in the development of splicing-switching therapies in particular for mutations that affect both splicing and protein function PMID: 27227676
11. This study confirms the high heterogeneity of molecular defects leading to hemophilia B in Belgium. Six missense variants and 1 in-frame deletion, previously unreported, were predicted to affect FIX protein function. PMID: 27865967
12. this study shows that targeted high-throughput sequencing is an effective technique to detect the F9 gene mutations in hemophilia patients PMID: 27292088
13. Patient 1 had a 149-kb deletion with breakpoints 90-kb upstream and 30-kb downstream from F9. Patients 2 and 3 showed 273-kb and 1.19-Mb deletions respectively. Patient 4 had two deleted regions: a 1663-bp deletion 1.34-Mb upstream from F9 and a 7.2-Mb deletion including F9. PMID: 26686734
14. Factor IX mutation was found in every family: eight had large deletions, three had small deletions (<10 base pair) and 102 had single base pair substitutions (69 missense, 26 nonsense, four splice site and three promoter). PMID: 26612714
15. Data suggest that coagulation factor IX (hFIX) minigene containing beta-globin (hBG) introns could represent a particular interest in stem cell-based gene therapy of hemophilias. PMID: 26928674
16. miR-128 and miR-125 could help to increase the nonsense-mutant F9 levels by repressing nonsense-mediated mRNA decay. PMID: 27133073
17. In 293T cells, the addition of 0.5 mM Ca(+2) and 1 mM Mg(+2) resulted in higher recombinant human Factor IX concentration. SK-Hep-1 cell line proved to be very effective in rhFIX production, and it can be used as a novel biotechnological platform for the production of recombinant proteins. PMID: 26802680
18. Mutations were revealed in 56 unrelated patients with hemophilia B in this study by using direct sequencing of factor IX gene functionally important fragments. PMID: 27529981
19. The Cys109Tyr F9 mutation found in two siblings and their mother, is a missense mutation previously described in two patients with hemophilia B, but first in Korea. PMID: 25402191
20. Differentiation studies demonstrated osteogenic (but not chondrogenic or adipogenic) differentiation capability and efficient FIX secretion of the enclosed MSCs in the fibronectin-alginate suspension culture. PMID: 24564349
21. Selective disruption of exosite-mediated regulation of factor IX by heparin and antithrombin can be achieved with preserved or enhanced thrombin generation capacity. PMID: 25851619
22. study revealed six unique and unreported changes in the F9 gene among haemophilia B patients from Macedonia and Bulgaria PMID: 25582609
23. We conclude that the nature of the F9 gene mutation may be an important risk factor for the development of inhibitors. PMID: 25470321
24. Activatable bioengineered FIX molecules with FVIII-independent activity might be a promising tool for improving hemophilia A treatment, especially for patients with inhibitors. PMID: 25224783
25. Data suggest that Gly317 plays role in normal catalytic function for FIX/FIXa in the clotting cascade; mutations in Gly317 (G317R, G317E) result in variable severity of bleeding in hemophilia B patients. PMID: 26023895
26. repetitive elements and non-B DNA forming motifs contribute to deletion mutations in severe haemophilia B PMID: 24816826
27. Various factor IX mutations have been identified in Chinese hemophilia B patients. PMID: 24261420
28. 11 FIX gene mutations (8 point mutations, 2 small deletions/insertions, and 1 large deletion), including two novel mutations (exon6 c.687-695, del 9 mer and c.460-461, ins T) were found. PMID: 24656159
29. Report oral FIX gene transfer strategy for hemophilia B. PMID: 24679056
30. This review discuss structural features of factor XIa that are required for factor IX activation, and the importance of the protease's dimeric structure. [review] PMID: 24759143
31. Circulating contact-pathway-activating microparticles together with factors IXa and XIa induce spontaneous clotting in plasma of hematology and cardiologic patients. PMID: 24498168
32. Thrombin-mediated, TAFI-dependent down-regulation of fibrinolysis provides new clues for explaining the heightened thrombotic risk in subjects carrying the FIX-Padua mutation. PMID: 24136406
33. 87 unique mutations (9 novel) were found in 225 American hemophilia B patients. c.316G>A, c.1025C>T, and c.1328T>A accounted 37.1%. Only those with large deletions and nonsense mutations had inhibitors. PMID: 24375831
34. The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. PMID: 24068708
35. The results suggest the Omega-loop of FIX binds to an area on FXIa composed of residues from the N-terminus and C-terminus of the A3 domain. These residues are buried in zymogen FXI, and must be exposed upon conversion to FXIa to permit FIX binding. PMID: 23617568
36. Report interactive database providing insights into mechanisms of hemophilia B. PMID: 23617593
37. Data indicate that five nanofilters can be used interchangeably to yield a high purity Coagulation Factor IX product. PMID: 23410583
38. Elevated factor IX activity is associated with an increased odds ratio for both arterial and venous thrombotic events. PMID: 24124147
39. Letter: report factor IX activity/antigen ratio in relation to risk of first unprovoked venous thromboembolism. PMID: 23446552
40. Mutations at the -5/-6 site (nucleotides -5 and -6 relative to the transcription start site, designated 1) of the F9 promotor account for the majority of hemophilia B Leyden cases and disrupt the binding of ONECUT transcription factors. PMID: 23472758
41. Results demonstrate the role of plasticity in regulating FIXa function with respect to discrimination of extended substrate sequences. PMID: 22212890
42. structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI. PMID: 23530052
43. Report causative F9 mutations in Argentine families with hemophilia B and determine mutation-associated FIX inhibitor risks. PMID: 23093250
44. The effect of surface contact activation and temperature on plasma coagulation with an RNA aptamer directed against factor IXa. PMID: 23054460
45. investigated the contribution of the NH2-terminal EGF-domain (EGF1) to the recognition specificity of intrinsic tenase by constructing an EGF1 deletion mutant and characterising the properties of the mutant in kinetic, direct binding and FRET assays PMID: 23014580
46. The results suggest that information at the mRNA level as well as conservation of amino acids of coagulation factor IX correlate well with disease severity. PMID: 22639855
47. Results indicate that fXIa activates fIX by an exosite- and Ca(2+)-mediated release-rebind mechanism. PMID: 22961984
48. Western blotting of plasma from FIX deficient (Hemophilia B) patients revealed traces of full-length FIX for the p.R294* and p.R298* mutations, but not for the p.L103* mutation that triggered major FIX mRNA decay. PMID: 22618954
49. factor IX mutations were identified in either the exon or intronic regions in haemophilia B patients in Malaysia; one novel mutation, 6660_6664delTTCTT was identified in siblings with moderate form of haemophilia B PMID: 22870602
50. The F9 mutations were heterogenous and the missense mutations were the most prevalent gene defects in Chinese haemophilia B patients. PMID: 22544209
顯示更多

收起更多
相關(guān)疾病：

Hemophilia B (HEMB); Thrombophilia, X-linked, due to factor IX defect (THPH8)
亞細(xì)胞定位：

Secreted.
蛋白家族：

Peptidase S1 family
組織特異性：

Detected in blood plasma (at protein level). Synthesized primarily in the liver and secreted in plasma.
數(shù)據(jù)庫鏈接：

HGNC: 3551

OMIM: 300746

KEGG: hsa:2158

STRING: 9606.ENSP00000218099

UniGene: Hs.522798

Most popular with customers

YWHAG Recombinant Monoclonal Antibody

Applications: ELISA, WB, IHC

Species Reactivity: Human
YWHAB Recombinant Monoclonal Antibody

Applications: ELISA, WB, IHC, IF, FC

Species Reactivity: Human, Mouse, Rat
Phospho-YAP1 (S127) Recombinant Monoclonal Antibody

Applications: ELISA, WB, IHC

Species Reactivity: Human
XRCC5 Recombinant Monoclonal Antibody

Applications: ELISA, WB, IHC, IF

Species Reactivity: Human
XPNPEP1 Recombinant Monoclonal Antibody

Applications: ELISA, IHC, FC

Species Reactivity: Human
WT1 Recombinant Monoclonal Antibody

Applications: ELISA, WB, IHC

Species Reactivity: Human
WFDC2 Recombinant Monoclonal Antibody

Applications: ELISA, WB, FC

Species Reactivity: Human
WDR5 Recombinant Monoclonal Antibody

Applications: ELISA, IHC, FC

Species Reactivity: Human