Recombinant Human Ficolin-3 (FCN3) Protein (His)

Name: Recombinant Human Ficolin-3 (FCN3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02069P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Human Ficolin-3 (FCN3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O75636
Target Symbol	FCN3
Synonyms	FCN3; FCNH; HAKA1; Ficolin-3; Collagen/fibrinogen domain-containing lectin 3 p35; Collagen/fibrinogen domain-containing protein 3; Hakata antigen
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	QEHPSCPGPRELEASKVVLLPSCPGAPGSPGEKGAPGPQGPPGPPGKMGPKGEPGDPVNLLRCQEGPRNCRELLSQGATLSGWYHLCLPEGRALPVFCDMDTEGGGWLVFQRRQDGSVDFFRSWSSYRAGFGNQESEFWLGNENLHQLTLQGNWELRVELEDFNGNRTFAHYATFRLLGEVDHYQLALGKFSEGTAGDSLSLHSGRPFTTYDADHDSSNSNCAVIVHGAWWYASCYRSNLNGRYAVSEAAAHKYGIDWASGRGVGHPYRRVRMMLR
Expression Range	24-299aa
Protein Length	Full Length of Mature Protein
Mol. Weight	34.4 kDa
Research Area	Immunology
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	May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota.
Subcellular Location	Secreted. Note=Found in blood plasma, bronchus, alveolus and bile duct.
Protein Families	Ficolin lectin family
Database References	HGNC: 3625 OMIM: 604973 KEGG: hsa:8547 STRING: 9606.ENSP00000270879 UniGene: PMID: 29491225 Study found the ratio of ficolin-3/adiponectin at 16-18 weeks of gestation was changed in pregnant women who subsequently developed gestational diabetes mellitus GDM, and might provide effective early predicting and screening for GDM. PMID: 28445618 Ficolin-3 was overexpressed in the serum of most hepatocellular carcinoma patients after Radiofrequency ablation . Ficolin-3 might be a biomarker for Radiofrequency ablation treatment efficacy and a potential target for hepatocellular carcinoma immunotherapy. PMID: 29386009 Serum H-ficolin levels inversely correlated with ground-glass opacity score on chest computed tomography in systemic sclerosis-interstitial lung disease (SSc-ILD) patients. H-ficolin-related innate immunity may be involved in SSc-ILD development. PMID: 28432700 Ficolin-3 plasma levels are associated with the presence and progression of abdominal aortic aneurysm (AAA), suggesting its potential role as a biomarker of AAA PMID: 28039962 results suggest that anti-ficolin-3 antibodies could be useful for the diagnosis of active nephritis in SLE patients PMID: 27631981 this study shows that H-ficolin may aid clearance of influenza A virus by promoting monocyte uptake of the virus, while reducing viral replication and virus-induced TNF-a responses in these cells PMID: 27856789 These results suggest that polymorphisms in the FCN3 gene cooperate to increase ficolin-3 concentration and that it might contribute to leprosy susceptibility by favoring Mycobacterium leprae infection. PMID: 28241035 subjects that were heterozygote carriers of both FCN2 + 6424 and FCN3 + 1637delC were sufficient mannan-binding lectin producers PMID: 26795763 in patients with systemic lupus erythematosus, there was no significant association between ficolin-1 and ficolin-3 with lupus nephritis PMID: 27981461 Monitoring serum H-ficolin levels was shown to be of no benefit in terms of predicting severe infection. PMID: 26377840 Serum levels of ficolin-2 and ficolin-3 were significantly lower in the cardiac syndrome X patients compared to controls. PMID: 27312152 LPS induces a tissue-specific recruitment of ficolin-3 and ficolin-1 in the lung and systemic compartment, respectively, suggesting an important role of distinct lectin complement pathway initiators in the local pulmonary and systemic host defence. PMID: 26868430 Lower serum ficolin-3 levels were correlated with injury severity following traumatic brain injury. PMID: 26627059 this study provide novel insight in the binding and complement activating capacity of the lectin pathway initiation molecules ficolin-2 and ficolin-3 towards relevant Gram-negative pathogens of pathophysiological relevance. PMID: 26074063 Data indicate differences in the plasma concentrations of collectin liver 1 and collectin kidney 1, M-ficolin and H-ficol in systemic lupus erythematosus (SLE) patients compared to a group of healthy controls. PMID: 26154564 H-ficolin participates in A. fumigatus defence through the activation of the lectin complement pathway, enhanced fungus-host interactions and modulated immune responses. PMID: 26133042 data suggest that high levels of the complement activating molecule H-ficolin are associated with an increased risk of future progression to microalbuminuria in patients with newly diagnosed type 1 diabetes. PMID: 25064124 High ficolin-3 level at the time of transplantation was an independent significant risk factor for shorter graft survival. PMID: 25222012 There is lack of association of serum mannose-binding lectin or ficolins with complement activation in patients with antiphospholipid antibodies. PMID: 25083730 This study aims to investigate whether an association exists between the ficolins that are part of the lectin complement pathway and systemic lupus erythematosus. PMID: 25069872 Both ficolin-3 and MASP-2 levels correlated inversely with the time from the onset of the attack of hereditary angioedema until blood sampling PMID: 25042985 Data show that the plasmid pETb-ficolin 3 was cloned successfully and the purity of the protein His-ficolin 3 was over 90%. PMID: 25001927 Data show that the expression of ficolin-3(FCN3) in ovarian cancer (OC) was inversely correlated with serum ficolin-3 and lower in comparison with controls. PMID: 23744477 low levels of ficolin-3 are associated with advanced heart failure and outcome. The decrease of ficolin-3 was associated with increased complement activation. PMID: 23596511 Increased fucosylation of ficolin 3 in plasma of the rheumatoid arthritis patients PMID: 23107985 Survival analyses showed that high pre-transplant serum levels of FCN3 were associated with decreased graft survival, suggesting an important role of FCN3 in the pathophysiology of kidney graft rejection PMID: 23416240 Data indicate that the median concentration of MASP-2/ficolin-3 complexes was 119.7 AU/ml (range: 2.9-615.5 AU/ml). PMID: 23142462 Both pre-term deliveries and low birth weight (independently of gestational age) were significantly associated with low H-ficolin concentrations but not with heterozygosity for the FCN3 1637delC frameshift mutation. PMID: 22226667 Found that a common variant of FCN3/CD164L2 is associated with hypertension in Chinese population. PMID: 22471352 H-ficolin has antiviral activity against influenza A virus (IAV). H-ficolin also fixes complement to a surface coated with IAV. PMID: 22851708 The purpose of this study was to determine whether circulating levels of ficolin-2 and ficolin-3 are altered in normal pregnancy and pre-eclampsia. PMID: 22670778 Cord blood MBL concentrations were significantly lower in intrauterine-growth-restriction (IUGR) cases than controls. No differences in H- and L-ficolin concentrations were observed between groups. PMID: 22082351 in whole serum. MASP-2 was co-purified with H-ficolin, and the purified H-ficolin.MASP-2 complex could activate complement as measured by cleavage of complement factor C4 PMID: 22238349 Data indicate that the deposition of both C4 and C3 showed a significant positive correlation with the serum concentration of Ficolin-3. PMID: 21085669 MBL-associated serine protease-3 down-regulate Ficolin-3 mediated complement activation through the lectin pathway. PMID: 19939495 Hakata antigen, a ficolin associated with MBL-associated serine proteases and small MBL-associated protein, activates the lectin complement pathway. PMID: 11907111 Hakata circulates as Hakata-MASPs complex in the blood, binds Aerococcus viridans polysaccharide and inhibits A. viridans growth PMID: 12367778 The X-ray structures of H-ficolin trimeric recognition domains, alone and in complex with various ligands, have been solved. PMID: 17215869 variations in H-ficolin appear to be of limited importance in the pathogenesis of Crohn's disease PMID: 17303612 Ficolin 3 mediates the clearance of late apoptotic cells, which suggests that this protein is involved in the maintenance of tissue homeostasis and might play a protective role against the development of autoimmunity. PMID: 17469142 Ficolin-3 has a high complement activating potential and is the only collagenase proteolytic resistant molecule among the lectin complement pathway initiators. PMID: 18006063 an FCN3+1637delC deletion variant disrupting the possibility for pattern recognition was detected; characterization of recombinant variant Ficolin-3 shows that homozygosity for the FCN3+1637delC deletion may lead to Ficolin-3 deficiency PMID: 18261799 L-ficolin residue lysine57 is a key component of the interaction with both the mannan-binding lectin (MBL)-associated serine proteases and calreticulin, providing a strong indication that MBL and ficolins share homologous binding sites for their partners. PMID: 19109177 Results suggest that the elevation of S-ficolin-3 and its association with specific manifestations in systemic lupus erythematosus may indicate a pathogenetic role of ficolin-3 in SLE. PMID: 19208603

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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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