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anti-Human Factor VII Antikörper:
anti-Mouse (Murine) Factor VII Antikörper:
anti-Rat (Rattus) Factor VII Antikörper:
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Human Monoclonal Factor VII Primary Antibody für EIA, WB - ABIN951602
Kazama, Pastuszyn, Wildgoose, Hamamoto, Kisiel: Isolation and characterization of proteolytic fragments of human factor VIIa which inhibit the tissue factor-enhanced amidolytic activity of factor VIIa. in The Journal of biological chemistry 1993
Show all 4 Pubmed References
Human Polyclonal Factor VII Primary Antibody für IF (p), IHC (p) - ABIN1385638
Liu, Xue, Tang, Hou, Qi, Chen, Chen, Zhang, Chen, Xu: A simple method for isolating and culturing the rat brain microvascular endothelial cells. in Microvascular research 2013
Human Polyclonal Factor VII Primary Antibody für IHC (p), IHC - ABIN441425
Naderi: Coagulation factor VII is regulated by androgen receptor in breast cancer. in Experimental cell research 2015
Results suggest that inhibition of FVIIa with small-molecule active-site inhibitors represents a promising antithrombotic approach.
Hepsin plays a physiologically important role in factor VII activation and hemostasis in zebrafish.
study reports the full-length cDNA sequences of rhesus monkey FVII; deduced protein sequence of FVII indicates the functional domains; comparison of three-dimensional protein structure with human shows high conservation between them
our present data provide convincing evidence that FVIIa binding to EPCR elicits anti-inflammatory signaling via a PAR1- and beta-arrestin-1 dependent pathway.
Hemophagocytic lymphohistiocytosis and congenital factor VII deficiency caused by compound heterozygote mutations of Factor 7 were found in a 50-year old Chinese female patient. Her family members carried the same mutations but were asymptomatic. (Case reports)
This study demonstrates that -402G/A of FVII may be a risk factor for lower extremity deep venous thrombosis patients in a Chinese Han population.
The heterozygosity for MTHFR (rs1801133, rs1801131) and FVII (rs6046) polymorphisms, that could determine genetic predisposition to thrombosis, is high in Turkish Cypriot population.
there is a strong association between ApoC-III and FVIIa-AT levels in coronary artery disease
Coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase.
The unexplored newly formed interactions between EGF2 and TF provides a possible explanation for TF-induced allosteric activation of FVIIa.
TF-FVIIa/trypsin-mediated PAR2 activation leads to enhanced MMP-2 expression in human breast cancer cells contributing to tumor progression.
The current meta-analysis suggested that polymorphism of R353Q in factor VII was not associated with the MI risk.
The obtained results suggest a possible protective role of Gln353 and -122C alleles in Recurrent Miscarriage.
FVIIa-antithrombin levels in early and late preeclampsia
Using protein C-factor VII chimera demonstrate that APC light chain amino acid residues outside the EPCR-binding site enable cytoprotective PAR1 signaling.
model predicts that small vesicles promote activation of FX by the extrinsic tenase (VIIa/TF) significantly better than large vesicles
Low levels of FVII:C and FVIIa reflected the degree of consumption of the coagulation factor among paediatric sepsis patients with disseminated intravascular coagulation.
Report a good correlation between the type of F7 mutation and/or polymorphisms and FVII:C levels, without a direct link between FVII:C and bleeding tendency in factor VII deficiencies.
Polymorphism rs6046 of the FVII gene is associated with the development of fetal growth retardation in Central Russia.
A common pathogenic mechanism, possibly a defective folding of the mutant proteins, was triggered by the FVII mutations. The misfolded state led to impaired trafficking of these proteins causing Endoplasmic reticulum retention, which would explain the low to very low FVII plasma levels observed in patients carrying these mutations.
FVIIa-antithrombin but not FVIIa is a ligand for LRP1, and LRP1 contributes to the clearance of FVIIa-antithrombin in vivo
Data suggest that, for all coagulation proteins tested (prothrombin, factor X, activated factor VII, activated protein C), tighter binding to lipid bilayers (lower Kd) is observed as the proportion of anionic phospholipid increases. These studies were conducted in high-throughput screening using phospholipid bilayers in nanodiscs with multiplexed silicon photonic sensor (micro-ring resonator) array technology.
A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa complex activates FVIII apart from thrombin feedback.
Trancriptomic analysis shows that expression of the antithrombins serpin C1 and D1 is significantly reduced in Schwann cell-deficient mice. In the absence of peripheral neuromuscular activity, neurodegeneration is completely blocked, and expression of prothrombin in muscle is markedly reduced.
Leu8 is crucial for FVIIa-EPCR binding; this study characterizes its interaction in vivo in mice
FVIIa binding to EPCR leads to a barrier protective effect in vivo
FVIIa binding to EPCR on the endothelium facilitates the transport of FVIIa from circulation to extravascular tissues where TF resides
RNA interference of Serpinc1 and/or Proc allows for evaluation of the function of these genes in vivo and provides a novel, controlled mouse model for spontaneous venous thrombosis.
Murine FVIIa binds poorly to murine EPCR.
GlycoPEGylated rFVIIa (N7-GP) has a prolonged hemostatic effect in hemophilic mice compared with rFVIIa
Conclude that the fVII-targeted verteporfin photodynamic therapy that we report here is a novel and effective therapeutic with improved selectivity for the treatment of breast cancer.
The participation of Egr-1 in FVIIa-mediated regulation of keratinocyte function was confirmed by use of Egr-1-deficient mice, wherein a significant delay in skin wound healing after injury was observed, relative to WT mice.
Recombinant FVIIa readily associates with the vascular endothelium and subsequently enters into extravascular spaces where it is likely to bind to tissue factor and is retained for extended time periods.
Gene targeting of tissue factor, factor X, and factor VII in mice: their involvement in embryonic development
true circadian rhythms for FVII were found
Data suggest that long-term expression of murine activated factor VII is safe, but elevated levels cause premature mortality.
tissue factor/Factor VIIa/PAR2 signaling mediates neutrophil activation and fetal death in antiphospholipid syndrome and that statins may be a good treatment for women with aPL-induced pregnancy complications.
FVIIa functions in the asthmatic response to an allergen by stimulating lung eosinophilia, airway hyperresponsiveness, and mucin production.
Plasma elimination kinetics for factor VII are independent of its activation to factor VIIa and complex formation with plasma inhibitors.
Mice homozygous for the heparin-binding domain mutation R48C developed spontaneous, life-threatening thrombosis, occurring as early as the day of birth. Only 60% of the offspring reached weaning age, with further loss at different ages
in the heart, TF plays an important role in the thrombogenesis and it counterbalances AT-dependent anticoagulation; regulation of TF-procoagulant activity take place differently between the liver and the heart
This gene encodes coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. This factor circulates in the blood in a zymogen form, and is converted to an active form by either factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of the factor VII, a heavy chain containing a catalytic domain and a light chain containing 2 EGF-like domains are generated, and two chains are held together by a disulfide bond. In the presence of factor III and calcium ions, the activated factor then further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Defects in this gene can cause coagulopathy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
coagulation factor VII
, serum prothrombin conversion accelerator
, clotting factor
, FVII coagulation protein
, eptacog alfa
, anti-thrombin 3
, serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
, serpin C1
, serpin peptidase inhibitor, clade C, member 1