Recombinant Human Coagulation Factor Vii (F7) Protein (His-SUMO)

Name: Recombinant Human Coagulation Factor Vii (F7) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04130P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) F7.

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Product Overview

Description	Recombinant Human Coagulation Factor Vii (F7) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P08709
Target Symbol	F7
Synonyms	coagulation factor VII (serum prothrombin conversion accelerator); Coagulation factor VII; Eptacog alfa ; F7; FA7_HUMAN; Factor VII ; Factor VII heavy chain; Factor VII light chain; FVII coagulation protein ; OTTHUMP00000018733; OTTHUMP00000018734; Proconvertin; Serum prothrombin conversion accelerator; SPCA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGR
Expression Range	61-212aa
Protein Length	Partial
Mol. Weight	33.0kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 3544 OMIM: 227500 KEGG: hsa:2155 STRING: 9606.ENSP00000364731 UniGene: PMID: 29870887 The current meta-analysis suggested that polymorphism of R353Q in factor VII was not associated with the MI risk. PMID: 30278561 The obtained results suggest a possible protective role of Gln353 and -122C alleles in Recurrent Miscarriage. PMID: 27504943 FVIIa-antithrombin levels in early and late preeclampsia PMID: 28887028 model predicts that small vesicles promote activation of FX by the extrinsic tenase (VIIa/TF) significantly better than large vesicles PMID: 28935233 Low levels of FVII:C and FVIIa reflected the degree of consumption of the coagulation factor among paediatric sepsis patients with disseminated intravascular coagulation. PMID: 28492702 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. PMID: 28447100 Polymorphism rs6046 of the FVII gene is associated with the development of fetal growth retardation in Central Russia. PMID: 28544373 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. PMID: 29246447 FVIIa-antithrombin but not FVIIa is a ligand for LRP1, and LRP1 contributes to the clearance of FVIIa-antithrombin in vivo PMID: 27614059 heterozygotes for FVII deficiency show rare bleeding manifestations which are also present in the unaffected family members with normal FVII levels. This indicates that Factor VII activity levels played no role in the occurrence of the bleeding symptoms. Furthermore, FVII levels of around 0.40 IU/dl are capable of assuring a normal hemostasis. PMID: 28176610 plasma FVIIa-AT has a thrombophilic role in total and cardiovascular mortality risk in patients with clinically stable stable coronary artery PMID: 27061056 Family-based association study revealed that the G allele of Protein Z rs2273971, and haplotypes GA, CG, and CGA of Protein Z and factor VII had a significant effect on cerebral hemorrhage susceptibility. PMID: 27350683 Our study findings suggest a link between FVII and AR in prostate cancer pathogenesis. PMID: 27434295 Suggest that the hemostatic effect of pharmacological doses of rFVIIa in antibody-induced hemophilia mice stems from a TF-independent mechanism PMID: 26727350 Large deletions play a minor but essential role in the mutational spectrum of the F7 and F10 genes. Copy number analyses (e. g. MLPA) should be considered if sequencing cannot clarify the underlying reason of an observed coagulopathy. Of note, in cases of combined FVII/FX deficiency, a deletion of the two contiguous genes might be part of a larger chromosomal rearrangement. PMID: 26540129 Holders of the R allele had significantly higher activity of coagulation factor F7 (97.66 +/- 15.48 against 83.37 +/- 15.16, p = 0.002) and factor F2 (107.45 +/- 6.03 against 103.75 +/- 6.81, p = 0.023) than holders of the Q allele PMID: 27215039 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. PMID: 25828579 Decreased plasma levels of FVIIa in patients with deep vein thrombosis may indicate ongoing consumption of FVIIa and suggest a contributory role for TF in venous thrombus formation. PMID: 25891834 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. PMID: 25973586 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. PMID: 25767893 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. PMID: 24763923 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. PMID: 25104096 Polymorphism R353Q (coagulation factor VII) does not represent a protective or risk factor for acute myocardial infarction in young Mexican individuals PMID: 25393858 Two heterozygous mutations of F7, g.11349G>A and g.11482T>G, is associated with hereditary coagulation factor deficiency. PMID: 25863091 factor VIIa improved heat intolerance by attenuating hypothalamic neuronal apoptosis and damage. PMID: 25033928 Results show that the conformational allosteric activation signal extends to the EGF1 domain in the light chain of factor VIIa (FVIIa). PMID: 25344622 F7-323Ins10 was associated with lower factor VII levels, but not with individual intraventricular hemorrhage risk in preterm infants. PMID: 25179312 Decanucleotide insertion polymorphism of factor VII significantly influences the risk of thrombosis in patients with essential thrombocythemia. PMID: 24617727 High Coagulation factor VII expression is associated with breast cancer. PMID: 25447311 Persistently high levels of factor VII is associated with insulin resisitance. PMID: 24344794 The variability in Factor VII throughout the menstrual cycle in premenopausal women is no greater than for postmenopausal women or men. PMID: 24382103 The obtained results suggest a probable protective role of -323P10 allele against the risk of miscarriage in women with > or = 3 recurrent pregnancy losses. PMID: 25219139 plasma level is associated with ischemic stroke subtypes PMID: 24048512 Results suggest no association between R353Q polymorphism for factor VII and the presence or progression of coronary artery disease in the Iranian population. PMID: 24469878 Identification of a homozygous mutation in exon 8 of coagulation FVII that is responsible for factor VII deficiency in a Chinese pedigree. PMID: 23672839 Eight missense mutations were identified on the Factor 7 gene (p.Cys82Tyr, p.Cys322Ser, p.Leu357Phe, p.Thr410Ala, c-57C>T) PMID: 23731332 Data indicate that nanobilayers containing phosphatidic acid (PA) bound substantially more of two proteins, factor VIIa and activated protein C, than did equivalent bilayers containing phosphatidylserine (PS). PMID: 23879866 Data indicate that the interlaboratory precision was better for normal specimens than for factor VII (FVII) <20 U/dL with a mean coefficient of variation (CV) of 17.2% per specimen. PMID: 23590660 Polymorphisms in the coagulation factor VII gene modulate the susceptibility to coronary artery disease in Tunisian Arabs. PMID: 22932775 Rab GTPases regulate endothelial cell protein C receptor-mediated endocytosis and trafficking of factor VIIa. PMID: 23555015 elevated FVII levels, and the -323P0/10 but not R353Q polymorphism, constitute risk factors for ACS. PMID: 23275237 Data indicate that hfVII-LC and hIgG1-Fc can effectively inhibit tumor growth and metastases in SCID mice with tissue factor (TF) over-expressing colon cancer. PMID: 23494077 Data suggest that plasma FVIIa-AT complex (coagulation factor VII-antithrombin III) is higher in portal vein thrombosis (PVT; without cirrhosis) than in healthy subjects; no difference in FVIIa-AT complex is observed in cirrhosis with/without PVT. PMID: 22958499 Report comprehensive molecular analysis of FVII deficiency affected patients in North Tunisia. PMID: 22873696 Prothromin genetic mutatation is one of the risk factor in the development of venous thromboembolism and myocardial infarction. PMID: 23382263 glucose deprivation enhanced F7 expression in a mechanism reliant on prior ATF4 upregulation primarily due to increased transcription from the ATF4 gene. PMID: 22848420 rs6046A allele in F7 associated with decreased blood pressure levels (P PMID: 22815813 Intracellular depletion of GTP results in upregulation of coagulation factor VII. PMID: 23050902 functional analysis of lethal factor VII deficiency due to novel mutations in the F7 promoter reveals disruption of HNF4 binding site PMID: 22628013

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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