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F7 encodes coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. Additionally we are shipping Factor VII Kits (65) and Factor VII Proteins (31) and many more products for this protein.
Showing 10 out of 161 products:
Human Monoclonal Factor VII Primary Antibody for EIA, WB - ABIN951604
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 3 references for ABIN951604
Human Monoclonal Factor VII Primary Antibody for EIA, WB - ABIN951601
Bharadwaj, Iino, Kontoyianni, Smith, Foster, Kisiel: Factor VII central. A novel mutation in the catalytic domain that reduces tissue factor binding, impairs activation by factor Xa, and abolishes amidolytic and coagulant activity. in The Journal of biological chemistry 1997
Show all 3 references for ABIN951601
Human Polyclonal Factor VII Primary Antibody for 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 Monoclonal Factor VII Primary Antibody for EIA, RIA - ABIN452653
Takase, Tuddenham, Chand, Goodall: Monoclonal antibodies to human factor VII: a one step immunoradiometric assay for VII:Ag. in Journal of clinical pathology 1988
Hepsin (show HPN Antibodies) plays a physiologically important role in factor VII (show TH Antibodies) 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
FVIIa binding to EPCR (show PROCR Antibodies) leads to a barrier protective effect in vivo
FVIIa binding to EPCR (show PROCR Antibodies) on the endothelium facilitates the transport of FVIIa from circulation to extravascular tissues where TF resides
Murine FVIIa binds poorly to murine EPCR (show PROCR Antibodies).
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 (show EGR1 Antibodies) in FVIIa-mediated regulation of keratinocyte function was confirmed by use of Egr-1 (show EGR1 Antibodies)-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 (show F3 Antibodies) and is retained for extended time periods.
Gene targeting of tissue factor (show F3 Antibodies), factor X, and factor VII (show TH Antibodies) 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 (show TH Antibodies) is safe, but elevated levels cause premature mortality.
tissue factor (show F3 Antibodies)/Factor VIIa/PAR2 (show F2RL1 Antibodies) signaling mediates neutrophil activation and fetal death in antiphospholipid syndrome and that statins may be a good treatment for women with aPL (show FASL Antibodies)-induced pregnancy complications.
Structure-Function Relationship of the Interaction between Tissue Factor (show F3 Antibodies) and Factor VIIa.
Data suggest that allosteric regulation of FVIIa activity by tissue factor/thromboplastin (show F3 Antibodies) binding appear to involve direct interaction with FVIIa active site, stabilizing segment 215-217, activating loop 3, and leading to enhanced FVIIa activity.
The aim of the study was to evaluate the molecular basis behind low levels of FVII activity (FVII:C) levels in a cohort of Brazilian patients.
The story of FVII well summarizes the efforts of both theoretical and clinical approaches in the characterization of a coagulation disorder, that is, among the rare bleeding conditions, most frequently encountered in clinical practice.
Identified are the FVII gene mutations in the Chinese Han population of four unrelated FVII-deficient patients, and the effect of these mutations on the function of FVII molecule level has also been elucidated.
Molecular dynamics simulation of tissue factor (show F3 Antibodies) activation of factor VIIa.
results suggest that these TF residues interact with the GLA domain (show F9 Antibodies) of FX in a Mg(2 (show MUC7 Antibodies)+)-dependent manner (although effects of Mg(2 (show MUC7 Antibodies)+) on the FVIIa GLA domain (show F9 Antibodies) cannot be ruled out).
Describe inhibition of tissue factor:factor VIIa-catalyzed factor IX and factor X activation by TFPI (show TFPI Antibodies) and TFPI (show TFPI Antibodies) constructs.
Letter: large volume of distribution of rFVIIa explains the persistence of some clotting potential when FVII:C is no longer detectable in plasma of patients with inherited FVII deficiency.
Structural differences in the carboxyl-terminus between the inherited FVII and the therapeutic molecules contributed to the immune response. A naturally-occurring, poorly secreted and 5-residue truncated FVII (FVII-462X) escaped inhibition.
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
, clotting factor
, serum prothrombin conversion accelerator
, FVII coagulation protein
, eptacog alfa