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F8 encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation\; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. Additionally we are shipping Factor VIII Antibodies (253) and Factor VIII Kits (45) and many more products for this protein.
Showing 10 out of 26 products:
gene is flanked by factor VII (show TH Proteins) and factor X genes; gene encodes a protein homologous to factor VII (show TH Proteins), but lacks critical residues for factor VII (show TH Proteins) activity; functions as an inhibitor of blood coagulation in biochemical assays using zebrafish or human plasmas
data demonstrate that infusion of platelets containing FVIII triggers neither primary nor memory anti-FVIII immune response in FVIII(null) mice
Both platelet-VWF (show VWF Proteins) and plasma-VWF (show VWF Proteins) are required for optimal platelet-derived FVIII gene therapy for hemophilia A in the presence of inhibitors.
These data support the investigation of FVIII orthologs as treatment modalities in both the congenital and acquired FVIII inhibitor settings.
Activatable bioengineered FIX molecules with FVIII-independent activity might be a promising tool for improving hemophilia A treatment, especially for patients with inhibitors.
This study demonstrated that FVIIIa interacts with Low-density lipoprotein receptor-related protein 1 (show LRP1 Proteins) cluster III.
a fragment containing only approximately 20% of the VWF (show VWF Proteins) sequence is sufficient to support FVIII stability in vivo
Endothelial cells from multiple, but not all, tissues contribute to the plasma FVIII pool in the mouse.
Endothelial cells are the predominant, and possibly exclusive, source of plasma FVIII.
Micro-computed tomography analysis of distal tibia metaphyses also revealed for the first time a major impact of the FVIII/thrombin (show F2 Proteins)/PAR1 (show F2R Proteins) axis on the dynamic bone structure, showing reduced bone.
Findings indicate that improving protein trans-splicing by inter-chain disulfide bonding is a promising approach for increasing the efficacy of dual-vector based FVIII gene transfer.
Coagulation test results showed that the presence of double Glu113Asp, Arg593Cys mutations has a slightly synergistic effect on FVIII activity.
Report a dose-response relationship between high FVIII levels and risk of death in venous thrombosis patients and in individuals from the general population.
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.
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.
Interaction between VWF (show VWF Proteins) and FVIII in treating VWD (show VWF Proteins).
a grading system for FVIII mutations combining the severity determinants was developed and the grading pattern correlates with hemophilia phenotype, is reported.
Among the seven HA families whose coding region of the FVIII gene was directly sequenced,five patients and certain of their female relatives had mutations detected.
Stimulated GMVECs and HUVECs were found to secrete cell-anchored ultra-large VWF (show VWF Proteins) strings covered with bound FVIII.
Association between micro particle-tissue factor (show F3 Proteins) activity, factor VIII activity and recurrent VTE in patients with acute pulmonary embolism.
Using atomic force microscopy the study revealed a yet unknown Ca2 (show CA2 Proteins)+-dependent conformational change of the FVIII B-domain.
thrombin (show F2 Proteins) stimulates transglutaminase activity in articular cartilage by directly cleaving factor XIII (show UGDH Proteins) and by receptor-mediated up-regulation of factor XIII (show UGDH Proteins) synthesis
cupredoxin-like A1 subdomains in fVIII contain inter-species differences that are a result of selective pressure on the dissociation rate constant
Factor VIIIc (show COX7A2 Proteins) is responsible for tissue invasion during tumor progression.
This gene encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation\; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
, procoagulant component
, antihemophilic factor
, coagulation factor VIII
, coagulation factor VIIIc
, factor VIII F8B
, coagulation factor VIII, procoagulant component (hemophilia A)
, factor VIII
, coagulation co-factor