Recombinant Human Coagulation Factor Ix (F9) Protein (His-GST)

Name: Recombinant Human Coagulation Factor Ix (F9) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-07092P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Coagulation Factor Ix (F9) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P00740
Target Symbol	F9
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	FCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFP
Expression Range	144-239aa
Protein Length	Partial
Mol. Weight	42.0 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 3551 OMIM: 300746 KEGG: hsa:2158 STRING: 9606.ENSP00000218099 UniGene: PMID: 29724133 Report induced pluripotent stem cell model characterizing mutated F9 mRNA in hemophilia B. PMID: 28834196 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 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 a computational approach was conducted to select suitable location(s) for introducing new N-glycosylation sites into the human coagulation factor IX. PMID: 27356208 The pathogenic basis for one synonymous mutation (Val107Val) in the F9 gene associated with haemophilia B was determined. PMID: 28007939 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 Specific factor IX mRNA and protein features that favor drug-induced readthrough over recurrent nonsense mutations have been reported. PMID: 28196793 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 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 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 this study shows that targeted high-throughput sequencing is an effective technique to detect the F9 gene mutations in hemophilia patients PMID: 27292088 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 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 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 miR-128 and miR-125 could help to increase the nonsense-mutant F9 levels by repressing nonsense-mediated mRNA decay. PMID: 27133073 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 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 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 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 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 study revealed six unique and unreported changes in the F9 gene among haemophilia B patients from Macedonia and Bulgaria PMID: 25582609 We conclude that the nature of the F9 gene mutation may be an important risk factor for the development of inhibitors. PMID: 25470321 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 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 repetitive elements and non-B DNA forming motifs contribute to deletion mutations in severe haemophilia B PMID: 24816826 Various factor IX mutations have been identified in Chinese hemophilia B patients. PMID: 24261420 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 Report oral FIX gene transfer strategy for hemophilia B. PMID: 24679056 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 Circulating contact-pathway-activating microparticles together with factors IXa and XIa induce spontaneous clotting in plasma of hematology and cardiologic patients. PMID: 24498168 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 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 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 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 Report interactive database providing insights into mechanisms of hemophilia B. PMID: 23617593 Data indicate that five nanofilters can be used interchangeably to yield a high purity Coagulation Factor IX product. PMID: 23410583 Elevated factor IX activity is associated with an increased odds ratio for both arterial and venous thrombotic events. PMID: 24124147 Letter: report factor IX activity/antigen ratio in relation to risk of first unprovoked venous thromboembolism. PMID: 23446552 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 Results demonstrate the role of plasticity in regulating FIXa function with respect to discrimination of extended substrate sequences. PMID: 22212890 structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI. PMID: 23530052 Report causative F9 mutations in Argentine families with hemophilia B and determine mutation-associated FIX inhibitor risks. PMID: 23093250 The effect of surface contact activation and temperature on plasma coagulation with an RNA aptamer directed against factor IXa. PMID: 23054460 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 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 Results indicate that fXIa activates fIX by an exosite- and Ca(2+)-mediated release-rebind mechanism. PMID: 22961984 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 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 The F9 mutations were heterogenous and the missense mutations were the most prevalent gene defects in Chinese haemophilia B patients. PMID: 22544209

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.