Sequence in raw or FASTA format:
Homo sapiens coagulation factor VII (serum prothrombin conversion accelerator) (F7), transcript variant 1, mRNA.
|Sequence Information||ORF Nucleotide Sequence
|Vector||pcDNA3.1+-DYK or customized vector|
|Clone information||Clone Map|
|Tag on pcDNA3.1+-DYK||N terminal DYKDDDDK tags|
|ORF Insert Method||CloneEZ® Seamless cloning technology|
|RefSeq Version||NM_000131.4, 388890241|
|Organism||Homo sapiens (human)|
|Definition||Homo sapiens coagulation factor VII (serum prothrombin conversion accelerator) (F7), transcript variant 1, mRNA.|
|Product||coagulation factor VII isoform a preproprotein|
Summary: 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. [provided by RefSeq, May 2012].
Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (a).
Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. A downstream translational start codon is selected for this RefSeq based on its better conservation in mammalian species. An upstream in-frame start codon is also present and would result in a protein that is 15 aa longer at the N-terminus, but this start codon is poorly conserved and located within a protein-binding site identified in the promoter region, as described in PubMed: 8576177. Leaky scanning by ribosomes may allow translation initiation at the downstream start codon.
Order your protein of interest with our Guaranteed or It's Free Service now! For details, please click here.
|Title||Factor VII and protein C are phosphatidic acid-binding proteins .|
|Author||Tavoosi N, Smith SA, Davis-Harrison RL and Morrissey JH.|
|Journal||Biochemistry 52 (33), 5545-5552 (2013)|
|Title||Structural and functional studies of gamma-carboxyglutamic acid domains of factor VIIa and activated Protein C: role of magnesium at physiological calcium .|
|Author||Vadivel K, Agah S, Messer AS, Cascio D, Bajaj MS, Krishnaswamy S, Esmon CT, Padmanabhan K and Bajaj SP.|
|Journal||J. Mol. Biol. 425 (11), 1961-1981 (2013)|
|Title||Factor VII assay performance: an analysis of the North American Specialized Coagulation Laboratory Association proficiency testing results .|
|Author||Zantek ND, Hsu P, Refaai MA, Ledford-Kraemer M, Meijer P and Van Cott EM.|
|Journal||Int J Lab Hematol 35 (3), 314-321 (2013)|
|Title||A recombinant adenovirus vector encoding the light chain of human coagulation factor VII and IgG1 Fc fragment to targeting tissue factor for colorectal cancer immunotherapy in the mouse model .|
|Author||Rao B, Gao Y, Zhou Q, Xiao P, Xia S, Ma J, Luo J, Xiao T, Le S, Huang M and Wang J.|
|Journal||J. Cancer Res. Clin. Oncol. 139 (6), 1015-1023 (2013)|
|Title||Rab GTPases regulate endothelial cell protein C receptor-mediated endocytosis and trafficking of factor VIIa .|
|Author||Nayak RC, Keshava S, Esmon CT, Pendurthi UR and Rao LV.|
|Journal||PLoS ONE 8 (3), E59304 (2013)|
|Title||Functional characterization of the human factor VII 5'-flanking region .|
|Author||Pollak ES, Hung HL, Godin W, Overton GC and High KA.|
|Journal||J. Biol. Chem. 271 (3), 1738-1747 (1996)|
|Title||Detection of two missense mutations and characterization of a repeat polymorphism in the factor VII gene (F7) .|
|Author||Marchetti G, Patracchini P, Gemmati D, DeRosa V, Pinotti M, Rodorigo G, Casonato A, Girolami A and Bernardi F.|
|Journal||Hum. Genet. 89 (5), 497-502 (1992)|
|Title||Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male .|
|Author||O'Brien DP, Gale KM, Anderson JS, McVey JH, Miller GJ, Meade TW and Tuddenham EG.|
|Journal||Blood 78 (1), 132-140 (1991)|
|Title||Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine .|
|Author||Bjoern S, Foster DC, Thim L, Wiberg FC, Christensen M, Komiyama Y, Pedersen AH and Kisiel W.|
|Journal||J. Biol. Chem. 266 (17), 11051-11057 (1991)|
|Title||A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z .|
|Author||Iwanaga S, Nishimura H, Kawabata S, Kisiel W, Hase S and Ikenaka T.|
|Journal||Adv. Exp. Med. Biol. 281, 121-131 (1990)|
|Technical Manual||GenEZ ORF Clone Technical Manual|
Our customer service representatives are available 24 hours a day, Monday through Friday; please contact us anytime for assistance.