F10 undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts ...
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100 µL
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100 µL
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100 µg
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150 µL
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100 µL
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100 µg
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100 µL
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100 µg
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1 mg
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100 µg
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100 µg
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100 µL
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200 µg
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100 µL
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20 µL
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100 µL
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1 mg
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