Recombinant Human Coagulation Factor Xii (F12) Protein (His)

Name: Recombinant Human Coagulation Factor Xii (F12) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00368P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Coagulation Factor Xii (F12) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P00748
Target Symbol	F12
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	IPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTR
Expression Range	20-372aa
Protein Length	Partial
Mol. Weight	43.3 kDa
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	Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 3530 OMIM: 234000 KEGG: hsa:2161 STRING: 9606.ENSP00000253496 UniGene: PMID: 29587641 High levels of FXII activity are present in the plasma of multiple sclerosis patients during relapse. PMID: 27188843 defective FXII contact activation provides thromboprotection, excess activation underlies the swelling disorder hereditary angioedema type III. This review provides an overview of the molecular basis of FXII contact activation and FXII contact activation-associated disease states. PMID: 28346966 Accumulation of FXII in acute respiratory distress syndrome lungs may contribute to the release of pro-inflammatory mediators, regulating lung inflammation. PMID: 28816340 Data suggest that coagulation factor XII (FXII) homozygous p.Gly341Arg mutation, caused by consanguineous marriage, probably underlies the congenital FXII deficiency in the pedigree. PMID: 29419864 FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states PMID: 28743596 Results demonstrated that the composition of the solution and the surface properties of the material all contribute to the observation of contact activation, and the activation of FXII is not specific to anionic surfaces as has been long believed. PMID: 28514863 Report an independent association between FXII levels and the risk of hemorrhagic stroke in Swedish population. PMID: 28433996 analysis of how FXII reacts to surface materials, which can be applied to the activities of FXII in its natural environment [review] PMID: 27282310 beta-amyloid interacts with fibrinogen and factor XII. These interactions can lead to increased clotting, abnormal clot formation, persistent fibrin deposition, and generation of proinflammatory molecules. PMID: 28661939 Abeta activates FXII, resulting in FXI activation and thrombin generation in human plasma, thereby establishing Abeta as a possible driver of prothrombotic states PMID: 26613657 results support a model for induction of contact activation in which activity intrinsic to single-chain FXII initiates alphaFXIIa and alpha-kallikrein formation on a surface. alphaFXIIa, with support from alpha-kallikrein, subsequently accelerates contact activation and is responsible for the full procoagulant activity of FXII. PMID: 28069606 The XPNPEP2 c-2399A and the ACE insertion/deletion polymorphisms analyzed in a population of patients with hereditary angioedema with F12 mutation were not a major determinant of disease expression. PMID: 27788882 in the presence of platelet polyphosphate and the downstream substrate fibrin, alphaFXIIa is a highly efficient and favorable plasminogen activator. PMID: 27694320 6 different mutations, including 3 missense mutations (Gly341Arg, Glu502Lys and Gly542 Ser), 1 insertion (7142insertC) and 2 deletions (5741-5742 delCA and 6753-6755delACA), were identixFB01;ed on the F12 gene. Three of them (Gly341Arg, 5741-5742delCA and 6753-6755delACA) are reported here for the first time. PMID: 27003566 The present findings therefore suggest that homozygous FXII-HAE mutation status leads to a severe phenotype in females and males, and to an increased risk of manifest symptoms in the latter. PMID: 26392288 As the factor XII pathway specifically contributes to thrombosis but not to hemostasis, interference with this pathway provides a unique opportunity for safe anticoagulation that is not associated with excess bleeding. The review summarizes current knowledge on factor XII functions, activators and inhibitors. PMID: 25609114 It is concluded that F12-46C/T carriage acts as an independent modifier of hereditary angioedema due to C1-INH deficiency severity. PMID: 26248961 Active neutrophil extracellular traps formation can induce factor XII-mediated coagulation activation in patients with disseminated intravascular coagulation with poor prognosis. PMID: 26706311 findings suggest that the three mutations in the F12 gene are the causing reasons for the cross-reactive material-negative FXII deficiencies PMID: 26709783 Results report first report of FXii mutation causing angioedema in a Brazilian family with normal CI inhibitor status. PMID: 25816745 Results support the importance of contact activation pathway-dependent TG as a risk factor for ischemic stroke, and indicate the importance of F12 SNPs for TG ex vivo and in vivo. PMID: 26286125 Genotyping these subjects revealed that the carriers of the minor alleles at the two loci- F12 and KLKB1 had a significant association with reduced levels of active plasma renin. PMID: 26969407 The results provide an essential basis for the diagnosis of FXII deficiencies in Chinese. PMID: 26105808 We postulate that FXIIa first strengthens the clot structure during clot formation and thereafter contributes towards fibrinolysis. PMID: 26153047 Women with low FXII level might have an increased risk of premature delivery at < 34 GW. PMID: 25879167 Provide the structural basis for understanding FXII substrate recognition and zymogen activation. PMID: 25604127 data illustrate a critical role for polyphosphate/factor XII-triggered coagulation in prostate cancer-associated thrombosis with implications for anticoagulation without therapy-associated bleeding in malignancies PMID: 26153520 the results of this study characterize the mechanism of HAEIII and establish FXII inhibition as a potential therapeutic strategy to interfere with excessive vascular leakage in HAEIII PMID: 26193639 influence of FXII 46C/T on further pregnancy outcomes PMID: 25489738 Suggest C1-inh polymers activate the FXII-dependent kallikrein-kinin system in hereditary angioedema. PMID: 25800206 The heterozygous mutation of g.8597G>A identified in exon 13 of FXII gene is associated with hereditary coagulation factor XII deficiency. PMID: 26037346 an F12 mutation is the principal FXII-HAE predictor, with the disease expression influenced by individual variations in kinin degradation enzyme activities. PMID: 25134986 Authors report for the first time in Brazil a mutation in the F12 gene as a likely cause of HAE with normal C1-INH in patients with recurrent attacks of angioedema and/or abdominal pain. PMID: 25790805 In a cohort with hereditary angioedema, four families carried the p.Thr309Lys mutation in F12 gene. PMID: 25744496 Abeta42-mediated contact system activation is driven by factor XII and can occur in the AD circulation PMID: 25775543 Heparan sulfate enhances FXIIa binding capacity and consequently migration of human lung fibroblasts isolated from fibrotic lungs. PMID: 25589788 we identified the 72-bp F12 deletion in two Turkish women with hereditary angiodema-FXII. The mutation was located at the exon 9/intron 9 border and involved the proline-rich region of the factor XII protein (FXII. PMID: 25113305 FXIIa was increased three-fold in ESRD patients relative to control plasma. After conversion to nocturnal hemodialysis, both DeltaMAP and DeltaTPR correlated with DeltaFXIIa. PMID: 24733030 In hypercortisolemic patients, no significant disorders are present concerning FXII concentrations due to the C46T polymorphism of its gene promoter. PMID: 24691729 FVIIa- and FXIIa-triggered coagulation pathways have distinct but complementary roles in atherothrombus formation. PMID: 24855058 [review] As it forms, activated factor XII converts prekallikrein (PK) to kallikrein; kallikrein cleaves high-molecular-weight kininogen to release bradykinin. PMID: 24388213 Data suggest factor XII binding/autoactivation are increased on surface of hantavirus-infected vascular endothelium; thus, activation of kallikrein-kinin system during hantavirus infection could have profound implications on capillary permeability. PMID: 23874198 Generated a specific and potent FXII/FXIIa aptamer anticoagulant that offers targeted inhibition of discrete macromolecular interactions involved in the activation of the intrinsic pathway of blood coagulation. PMID: 23692437 Using different coagulation assays, it was shown that platelet contribution to whole blood coagulation was unrelated to the generation of activated FXII in vitro. PMID: 23896408 Mutation in the F12 gene is a prerequisite for the expression of hereditary angioedema disease symptoms, but other factors may have protective or aggravating effects on clinical features. PMID: 23849223 These results may confirm the importance of the proline-rich region of factor XII protein in edema formation PMID: 23994767 Immobilized Ni(2+) and Cu(2+) bind FXII, FXI and high molecular weight kininogen with high affinity and stimulate activation of the contact pathway, driving FXII-mediated coagulation. PMID: 22905925 the F12 46TT genotype is strongly associated with cerebral venous thrombosis in the south Indian population PMID: 22500857 The goal of this review is to summarize the in vivo functions of FXII, with special focus to its functions in thrombosis and vascular biology. PMID: 22993391

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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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