Recombinant Human F8 Protein

Beta LifeScience SKU/CAT #: BL-2924PL

Recombinant Human F8 Protein

Beta LifeScience SKU/CAT #: BL-2924PL
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Product Overview

Tag N/A
Host Species Human
Accession P00451
Synonym F8, AHF, DXS1253E, F8B, F8C, FVIII, HEMA, coagulation factor VIII
Background Factor VIII (FVIII) is an essential blood-clotting protein, also known as anti-hemophilic factor (AHF). In humans, factor VIII is encoded by the F8 gene. Defects in this gene result in hemophilia A, a recessive X-linked coagulation disorder. Factor VIII is produced in liver sinusoidal cells and endothelial cells outside the liver throughout the body. This protein circulates in the bloodstream in an inactive form, bound to another molecule called von Willebrand factor, until an injury that damages blood vessels occurs. In response to injury, coagulation factor VIII is activated and separates from von Willebrand factor. The active protein (sometimes written as coagulation factor VIIIa) interacts with another coagulation factor called factor IX. This interaction sets off a chain of additional chemical reactions that form a blood clot.
Description Recombinant Human Antihemophilic Facor 8 produced in CHO is a glycosylated polypeptide chain having 2,322aa. The Factor-VIII protein is purified using our unique purification techniques.
Source CHO
Purity >97.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg of F8 protein by the LAL method.
Bioactivity The specific activity of Factor 8 protein was found to be 7,058 IU/mg.
Formulation Recombinant F8 protein was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.
Usage For Research Use Only
Storage Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

Target Details

Target Function Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa.
Subcellular Location Secreted, extracellular space.
Protein Families Multicopper oxidase family
Database References
Associated Diseases Hemophilia A (HEMA)

Gene Functions References

  1. This study describes an original pathological mechanism by which a small intronic deletion in F8 leads to Alu exonization. PMID: 29357978
  2. A common polymorphism decreases LRP1 mRNA stability and is associated with increased plasma factor VIII levels PMID: 28431990
  3. F8 and F9 gene variants result from a founder effect in two large French haemophilia cohorts PMID: 29656491
  4. our results demonstrate that the N-glycosylation sequon in the A2 domain is located in a structural element that is critically required for proper folding and conformation of FVIII. PMID: 28327546
  5. The aim of this study was to determine the F8 mutations in severe HA (sHA) patients and female carriers PMID: 29938987
  6. Human FVIII gene transfer without in vivo selection of manipulated cells can introduce immune tolerance in hemophilia A mice and this immune tolerance is CD4(+) T cell mediated. PMID: 28799202
  7. In Factor VIII, 41 mutations were identified, 19 of which were novel and 80% (44/55) of the pathogenic mutations fell into the categories of missense, nonsense(16.36%), frameshift (14.55%), and splice (5.45%) mutations. PMID: 28252515
  8. High dose of rhFVIII induces apoptosis in FVIII-specific memory B-cells but does not influence FVIII-specific T cell response. PMID: 28492697
  9. the potential role of FXIII-A in wound healing, as a field with long-term therapeutic implications, is also discussed PMID: 28894750
  10. Case Report: complex recombination with deletion in the F8 and duplication in the TMLHE mediated by int22h copies during early embryogenesis in proband's mother. PMID: 28492696
  11. Report a diagnostic algorithm that can reliably identify pathogenic variants of factor 8/9 and von Willebrand factor and diagnose patients with hemophilia A, hemophilia B or von Willebrand disease. PMID: 27734074
  12. Each hFVIII vector was administered to FVIII knockout (KO) mice at a dose of 10(10) genome copies (GC) per mouse. Criteria for distinguishing the performance of the different enhancer/promoter combinations were established prior to the initiation of the studies. PMID: 28056565
  13. Relevance of ethnic differences in factor XIII activity on laboratory reference ranges. PMID: 28488800
  14. analysis of co-existing variants in both F8 and PTGS-1 genes in a three-generation pedigree of hemophilia A PMID: 27629384
  15. Potential mutations of the F8 gene were analyzed. PMID: 28777843
  16. FVIII endocytosis is driven by interaction with LRP1 PMID: 28558995
  17. Of special importance is the sequential formation of disulfide bonds with different functions in structural support of VWF multimers, which are packaged, stored and further processed after secretion. Here, all these processes are being reviewed in detail including background information on the occurring biochemical reactions. [review] PMID: 28139814
  18. The FVIII C1 domain contributes significantly to the immune response against FVIII in acquired and congenital hemophilia inhibitor patients. PMID: 28507083
  19. the existing epidemiologic investigations with an overview of the range of possible biochemical and immunologic mechanisms that may contribute to the different immune outcomes observed with plasma-derived and recombinant FVIII products. PMID: 28432221
  20. discuss potential mechanisms through which these intronic SNPs regulate ST3GAL4 biosynthesis and the activity that affects VWF and FVIII PMID: 27584569
  21. the half-life of VWF ( approximately 15 hours) appears to be the limiting factor that has confounded attempts to extend the half-life of rFVIII. PMID: 27587878
  22. results revealed localized vascular expression of FVIII and von Willebrand factor and identified lymphatic endothelial cell as a major cellular source of FVIII in extrahepatic tissues. PMID: 27207787
  23. NGS analysis has identified a large deletion of exon 2 of the F8 gene in a family affected with hemophilia A. PMID: 27984605
  24. the results indicate that residues in the C1 and/or C2 domains of factor VIII are implicated in immunogenic factor VIII uptake, at least in vitro Conversely, in vivo, the binding to endogenous von Willebrand factor masks the reducing effect of mutations in the C domains on factor VIII immunogenicity. PMID: 27758819
  25. Galectin-1 and Galectin-3 are novel-binding partners for human FVIII. Gal-1 binding can influence the procoagulant activity of FVIII. PMID: 27013611
  26. In general, NGS provides an effective approach to screen for different HA causing mutation types in the F8 gene. PMID: 27824209
  27. Our results confirm the rare event of Haemophilia A and haemophilia B in the same patient originating from two distinct genetic defects in F8 and F9 genes. PMID: 27824213
  28. although fVIII bound avidly to soluble forms of clusters II and IV from LRP1, only soluble cluster IV competed with the binding of fVIII to full-length LRP1, revealing that cluster IV represents the major fVIII binding site in LRP1. PMID: 27794518
  29. The FVIII B domain variants, p.D963N, p.S806T, p.G873D, p.H998Q and p.Q1225R may be considered as polymorphism or non-pathologic mutations in patients with Haemophilia A. PMID: 26915717
  30. In this meta-analysis, we have assessed the association between the FXIII-A Val34Leu polymorphism and intracerebral hemorrhage risk. The results of a combined analysis showed no significant association between the FXIII-A Val34Leu polymorphism and ICH risk in the overall population. The results of this meta-analysis suggest that the FXIII-A Val34Leu polymorphism is not associated with ICH risk in a Caucasian population. PMID: 27525858
  31. this study shows that targeted high-throughput sequencing is an effective technique to detect the F8 gene mutations in hemophilia patients PMID: 27292088
  32. F8 intron 22 inversions and SNP rs73563631 have roles in severe hemophilia A in unrelated families PMID: 26489971
  33. von Willebrand factor binds to the surface of dendritic cells and modulates peptide presentation of factor VIII. PMID: 26635035
  34. Desmopressin acetate increases F8 plasma concentration in patients with combined deficiency of factors V and VIII. PMID: 26599105
  35. 37 (70%) of the 53 had discordant antigen-activity ratio, majority of those mutations produced FVIII with low FVIII-specific activity. However, 4 (7.5%) of the 53 mutations produced higher specific activity of FVIII. It is possible that these mutations either produce a secretory defect or an increased metabolic turnover to account for the low levels of FVIII with these mutations. PMID: 25550078
  36. In situ genetic correction of F8 intron 22 inversion in hemophilia A patient-specific induced pluripotent stem cells has been described. PMID: 26743572
  37. Platelet-targeted FVIII gene therapy has higher therapeutic efficacy compared to factor VIII replacement therapy may be due to accelerated thrombin generation. PMID: 26453193
  38. Five int22h homologous copies at the Xq28 locus identified in intron22 inversion type 3 of the Factor VIII gene. PMID: 26653368
  39. Letter: report deep intronic variants of factor VII gene in hemophilia A. PMID: 26246214
  40. Carriers of Inv22 or Inv1 of F8 may be precisely detected with inverse-shifting PCR PMID: 27455009
  41. Factor VIII 3E6 antibody binding decreases the thermal motion behavior of surface loops in the C2 domain on the opposing face, thereby suggesting that cooperative antibody binding is a dynamic effect. PMID: 26598467
  42. 3030 SNPS, 31 Indels and a large, 497 kb, deletion were found among 2535 subjects from 26 different ethnic groups participating in the 1000 Genomes Project. PMID: 26383047
  43. Coagulation test results showed that the presence of double Glu113Asp, Arg593Cys mutations has a slightly synergistic effect on FVIII activity. PMID: 26057490
  44. Report a dose-response relationship between high FVIII levels and risk of death in venous thrombosis patients and in individuals from the general population. PMID: 26264493
  45. Case Report: P1809L mutation in A3 induced the conformational change in the FVIII molecule that hampered antigenic determinant(s) located in the C2 domain and might result in the inhibitor development. PMID: 26278069
  46. FVIII predicted venous thrombosis recurrence in a dose-response fashion, overall and in several subgroups, and is a strong candidate component of recurrence prediction tools. PMID: 26270389
  47. FXIII expression was upregulated in the airways of asthmatic patients after allergen exposure. PMID: 26525229
  48. Interaction between VWF and FVIII in treating VWD. PMID: 25605439
  49. large F8 rearrangements pose the highest risk, while missense mutations pose the lowest risk of inhibitor development in Indian hemophilia A patients PMID: 26897466
  50. Identify deep intronic variants in 15 haemophilia A patients by next generation sequencing of the whole factor VIII gene. PMID: 25948085


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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.

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