Recombinant Human Coagulation Factor X Protein (C-Fc)

Name: Recombinant Human Coagulation Factor X Protein (C-Fc)
Brand: Beta LifeScience
SKU: BL-0197NP
Availability: InStock

BL-0197NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Coagulation Factor X is produced by our Mammalian expression system and the target gene encoding Asn32-Lys488 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession	P00742
Synonym	Coagulation factor X; Stuart factor; Stuart-Prower factor
Gene Background	F10, also known as Coagulation factor X, belongs to the peptidase S1 family that is synthesized as a 488 amino acid (aa) with a signal peptide and a pro region (residues 1‑40). Both the intrinsic and extrinsic pathways activate Factor X to Xa, which consists of light (residues 41‑179) and heavy (residues 235‑488) chains linked by a disulfide bond. Coagulation factor X is initially synthesized in the liver. The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5. F10 is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Molecular Mass	78.2 KDa
Apmol Mass	80-120&25 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM MES, 150mM NaCl, 0.2mM CaCl2, pH 5.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 3528 OMIM: 227600 KEGG: hsa:2159 STRING: 9606.ENSP00000364709 UniGene: Hs.361463
Associated Diseases	Factor X deficiency (FA10D)
Tissue Specificity	Plasma; synthesized in the liver.

Gene Functions References

An antidote could promptly neutralize the anticoagulant effects of both FXa inhibitors. Our results suggest that drugs and aptamers with shared targets can be combined to exert more specific and potent effects than either agent alone PMID: 29863725
model predicts that small vesicles promote activation of FX by the extrinsic tenase significantly better than large vesicles PMID: 28935233
miR-24 was overexpressed in major trauma-induced coagulopathy (TIC) patients. The negative correlation of miR-24 with FX suggested the possibility that miR-24 might inhibit the synthesis of FX during TIC. PMID: 28694557
zymogen-like factor Xa variants are conformationally dynamic and ligands such as its cofactor, factor Va, stabilize the molecule rescuing procoagulant activity. At the site of vascular injury, the variants in the presence of factor Va serve as effective prohemostatic agents. PMID: 28692575
Data suggest oxidized lipid vesicles with phosphatidylserine/polyunsaturated fatty acids promote inactivation of ZPI-PZ complex or free ZPI; binding of PZ-complexed or free ZPI to oxidized vesicles mediates inactivation of ZPI (an inhibitor of FXa); blocking heparin- (anticoagulant-)binding site on ZPI interferes with binding to lipid or PZ. (ZPI = protein Z-dependent protease inhibitor; PZ = protein Z; FXa = factor Xa) PMID: 28717005
PTX2 was identified PTX2 as a novel partner for FX, and both proteins cooperated to prevent their SR-AI-mediated uptake by macrophages. PMID: 28213380
annexin A2 contributes to lung injury and fibrotic disease by mediating the fibrogenic actions of FXa. PMID: 28283478
A family with factor X deficiency from Argentina displayed a compound heterozygous proband having the combination of a new mutation with an already known one, and homozygous children. PMID: 27031279
analysis of how physiological concentrations of Tissue factor pathway inhibitor inhibit FXa PMID: 26607136
According to our study, compounds 1a, 1g and 1s displayed evident FXa inhibitory activity and excellent selectivity over thrombin in in vitro inhibition activities studies. PMID: 27089317
This study was conducted to assess the spectrum of factor X gene mutation in Iranian patients with congenital factor X deficiency (FXD). Most molecular studies found a diversity in factor X disease causing mutations in Iranian patients. Like other parts of the world, the majority of mutations in Iranian patients were missense mutations, but splice-site mutations were relatively common. [review] PMID: 26891460
The Ala275Val substitution is a pathogenic mutation that causes the inherited FX deficiency. PMID: 26708756
homozygous mutation g.27881G>A(p.Val298Met) of the F10 gene has been identified, which probably accounts for the low FX concentrations in this pedigree PMID: 27264807
FX carboxyl-terminal region downstream of residue K467 is not essential for secretion and provides a modest contribution to pro-coagulant properties. PMID: 26083275
In our medical center, rivaroxaban concentrations could be assessed by a rapid chromogenic method. PMID: 26058941
FXa may inhibit lipopolysaccharide-mediated expression of sPLA2-IIA by suppression of cytosolic phospholipase A2 and extracellular signal-regulated kinase 1/2. PMID: 25399323
Several members of a family had a c.112 G>C mutation in exon 2 of the F10 gene. Although in-silico analysis predicts this is a benign mutation, this family suggests that the amino acid substitution affects the properties of the factor X protein. PMID: 25803519
Various acylcarnitines inhibited factor Xa-initiated clotting. PMID: 26175037
Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation. PMID: 26012870
The model of human prothrombinase presented here provides a powerful resource for contextualizing previous data and for designing future experiments PMID: 25153592
Factor Xa plasma levels were higher in shift work nurses compared to daytime working nurses. PMID: 25743687
Asp-185 deletion in FX predisposes FX deficient patient to mild bleeding phenotype. The catalytic activity of the recombinant mutant protease is severely impaired. PMID: 25179519
Factor Xa has a role in inhibiting HMGB1-induced septic responses in human umbilical vein endothelial cells and in mice PMID: 25007770
procoagulant, tissue factor-bearing microparticles in bronchoalveolar lavage of interstitial lung disease patients PMID: 24777000
Letter/Case Report: demonstrate the clinical utility of monitoring rivaroxaban levels through measurements of anti-Xa activity. PMID: 25688138
The results suggest that the mutation FX-M402T may cause a secretion defect and a molecular abnormality in FX. PMID: 25064371
Prothrombin is proteolytically converted by factor Xa to the active protease thrombin in a reaction that is accelerated >3,000-fold by cofactor Va. PMID: 24821807
High FXa expression is associated with vascular inflammation in sickle cell disease. PMID: 24449213
factor Xa induces an inflammatory signalling by activation of protease-activated receptors in human atrial tissue PMID: 24041930
Protein Z/protein Z-dependent protease inhibitor and Fxa expression in human gastric cancer cells indicate that these proteins may play a role in anticoagulant events at the tumor tissue. PMID: 24158387
The structure of factor Xa is regulated by factor Va and phosphatidylserine. PMID: 24467409
deficiency is associated with bleeding due to poor recognition of the mutant substrate by Factor IXa PMID: 23677006
In carotid artery plaque, expression of SPHK1 was observed at smooth muscle cell-rich sites and was co-localized with intraplaque FX/FXa content. PMID: 23658376
Seven missense mutations were identified in the F10 of the four probands with FX deficiency, six of which (Ser425Pro, Ala-29Pro, Phe324Leu, Ala235Thr, Cys111Arg and Met362Thr) were novel and associated with type I FX deficiency. PMID: 23664564
Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency. PMID: 24124146
A novel function for AT, which accelerates the modulation of FXa into the fibrinolytic form. PMID: 23416531
Despite their delay in reaching therapeutic anti-FXa levels on unfractionated heparin treatment, infants monitored with the adult-based anti-FXa range have a high thrombus resolution rate, no thrombus progression, but a relatively high bleeding rate. PMID: 22244010
We report two novel causative mutations of the Factor 10 gene in a Chinese proband with severe Factor X deficiency and mild clinical symptoms. PMID: 22931370
The Kunitz 1 and Kunitz 3 domains of tissue factor pathway inhibitor are required for efficient inhibition of factor Xa PMID: 22627666
results suggest that FX binds to the surface of human species C adenovirus and becomes a pathogen-associated molecular pattern that, upon viral entry into the cell, triggers activation of innate immunity PMID: 23019612
Three unrealted Palestinian patients were found to be homozygous for c302delG, a new frameshift mutation in the F10 gene causing a stop codon at amino acid 73. PMID: 22008904
srxA and prxA (2-Cys peroxiredoxin) genes are induced in response to oxidative stress. PMID: 21651559
patients with hypomethylated F10 promoter in tumors had shorter median overall survival PMID: 22160665
RXA plasma levels can be quantified accurately and precisely by a chromogenic anti-FXa assay on different coagulometers in different laboratories. PMID: 21840043
localization of PZ/ZPI and FX in colon cancer cells indicates that PZ/ZPI may contribute to anticoagulant events at the tumor site. PMID: 22424030
Alboserpin emerges as an atypical serpin that targets FXa and displays unique phospholipid specificity. PMID: 21673107
The regulatory action of FXa on PAR-2 was concentration-dependent and mimicked by a PAR-2-selective activating peptide. PMID: 21871560
Differential effects of murine and human factor X on adenovirus transduction via cell-surface heparan sulfate. PMID: 21596747
Determination of rivaroxaban by different factor Xa specific chromogenic substrate assays: reduction of interassay variability. PMID: 21811937
Six FXIa catalytic domain residues (Glu(98), Tyr(143), Ile(151), Arg(3704), Lys(192), and Tyr(5901)) were subjected to mutational analysis to investigate interactions between FXIa and a synthetic substrate, the substrate factor IX, and inhibitor PN2KPI. PMID: 21778227

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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.

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