Code | CSB-YP007932HU |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP007932HU-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
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Code | CSB-BP007932HU |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP007932HU |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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Coagulation factor VIII (FVIII, F8C) is a crucial protein involved in the process of hemostasis, playing an essential role in blood clotting [1]. It is a high molecular weight protein with platelet-aggregating activity, closely associated with a lower molecular weight subunit possessing factor VIII coagulant activity [2]. FVIII is an essential cofactor for the activation of factor X by factor IXa [3]. In plasma, FVIII is complexed with the von Willebrand factor (vWF) [4]. The FVIII protein consists of 2351 amino acids and is present as an inactive pro‐factor in the blood circulation [5]. It is synthesized primarily in endothelial cells and megakaryocytes [6]. The largest proportion of the FVIII/vWF complex is composed of von Willebrand Factor, found in endothelial cells, megakaryocytes, and platelets [7]. Studies have shown that FVIII is synthesized and released by cultured human endothelial cells [8].
References:
[1] C. Parmenter and S. Stoilova‐McPhie, "Binding of recombinant human coagulation factor viii to lipid nanotubes", Febs Letters, vol. 582, no. 12, p. 1657-1660, 2008. https://doi.org/10.1016/j.febslet.2008.04.018
[2] G. Vehar and E. Davie, "Preparation and properties of bovine factor viii (antihemophilic factor)", Biochemistry, vol. 19, no. 3, p. 401-410, 1980. https://doi.org/10.1021/bi00544a001
[3] G. Kemball‐Cook and E. Tuddenham, "The factor viii mutation database on the world wide web: the haemophilia a mutation, search, test and resource site hamsters update (version 3.0)", Nucleic Acids Research, vol. 25, no. 1, p. 128-132, 1997. https://doi.org/10.1093/nar/25.1.128
[4] K. Pflegerl, A. Podgornik, E. Berger, & A. Jungbauer, "Direct synthesis of peptides on convective interaction media monolithic columns for affinity chromatography", Journal of Combinatorial Chemistry, vol. 4, no. 1, p. 33-37, 2001. https://doi.org/10.1021/cc0100060
[5] A. Abdul-Ghafar, N. Bogdanova, L. Lim, Y. Zhao, A. Markoff, & S. Tien, "Ten novel factor viii (f8c) mutations in eighteen haemophilia a families detected in singapore", Haemophilia, vol. 16, no. 3, p. 551-553, 2010. https://doi.org/10.1111/j.1365-2516.2009.02146.x
[6] H. Yamane, N. Ochi, T. Tabayashi, L. Lu, T. Yamagishi, Y. Monobeet al., "Elevated coagulation factor viii plasma activity in a patient with lymphangiosarcoma", Internal Medicine, vol. 51, no. 22, p. 3213-3215, 2012. https://doi.org/10.2169/internalmedicine.51.8083
[7] S. Calvin, J. Corrigan, L. Weinstein, & M. Jeter, "Factor viii: von willebrand factor patterns in the plasma of patients with pre-eclampsia", American Journal of Perinatology, vol. 5, no. 01, p. 29-32, 1988. https://doi.org/10.1055/s-2007-999648
[8] E. Tuddenham, J. Lazarchick, & L. Hoyer, "Synthesis and release of factor viii by cultured human endothelial cells", British Journal of Haematology, vol. 47, no. 4, p. 617-626, 1981. https://doi.org/10.1111/j.1365-2141.1981.tb02691.x
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