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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 (342) and Factor VIII Kits (57) and many more products for this protein.
Showing 10 out of 22 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
Cytokine release was quantified from FVIII(-/-) splenocytes restimulated with FVIII in the absence or presence of different anti-FcgammaRIIB (CD32) Antibodies (anti-CD32 mAbs) over 6 days.
results revealed localized vascular expression of FVIII and von Willebrand factor (show VWF Proteins) and identified lymphatic endothelial cell as a major cellular source of FVIII in extrahepatic tissues.
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 (show VWF Proteins) masks the reducing effect of mutations in the C domains on factor VIII immunogenicity.
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.
A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa (show F10 Proteins) complex activates FVIII apart from thrombin (show F2 Proteins) feedback.
An in silico and in vitro approach to elucidate the impact of residues flanking the cleavage scissile bonds of FVIII by thrombin (show F2 Proteins) has been presented.
Of special importance is the sequential formation of disulfide bonds with different functions in structural support of VWF (show VWF Proteins) 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]
The FVIII C1 domain contributes significantly to the immune response against FVIII in acquired and congenital hemophilia inhibitor patients.
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.
discuss potential mechanisms through which these intronic SNPs regulate ST3GAL4 (show ST3GAL4 Proteins) biosynthesis and the activity that affects VWF (show VWF Proteins) and FVIII
the half-life of VWF (show VWF Proteins) ( approximately 15 hours) appears to be the limiting factor that has confounded attempts to extend the half-life of rFVIII.
Our finding that the C2-domain of FVIII can be replaced by that of FV without compromising FVIII activity may have translational implications.
It was concluded that VEGF and factor VIII are important growth factors associated with fetal development in pigs and are identified in all uterine segments.
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