Recombinant Human Complement Factor H (CFH) Protein (His)

Name: Recombinant Human Complement Factor H (CFH) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06274P
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 Complement Factor H (CFH) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P08603
Target Symbol	CFH
Synonyms	(H factor 1)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	EDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCS
Expression Range	19-449aa
Protein Length	Partial
Mol. Weight	50.5 kDa
Research Area	Cancer
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	Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed.
Subcellular Location	Secreted.
Database References	HGNC: 4883 OMIM: 126700 KEGG: hsa:3075 STRING: 9606.ENSP00000356399 UniGene: PMID: 29579408 Functional characterization of disease-associated genetic variants in the complement factor H gene in atypical hemolytic uremic syndrome and C3-glomerulopathy patients. PMID: 28941939 Evasion of C3b deposition at division septa and lateral amplification underneath the capsule requires localization of the FH-binding protein PspC at division sites. PMID: 30139996 These findings reveal that the CRP- and PTX3-binding characteristics of FHL-1 differ from those of FH, likely underpinning independent immune regulatory functions in the context of the human retina. PMID: 29374201 Two rare age-related macular degeneration-associated variants in the CFH gene (rs121913059 [p.Arg1210Cys] and rs35292876) deviate in frequency among different geographic regions. PMID: 29410599 these data demonstrate that Mesenchymal Stem Cells inhibit the activation of pathogenic C5 via up-regulation of FH, which improves our understanding of the immunomodulatory mechanisms of MSCs in the treatment of lupus nephritis. PMID: 29885865 Mutation in CFH gene is associated with age-related macular degeneration. PMID: 29686068 antioxidant and zinc nutritional supplement modifies risk of macular degeneration progression according to genotype PMID: 29311295 CC rs1061170 CFH genotype may be associated with the age-related macular degeneration. Additionally, CC rs1061170 CFH genotype may promote a negative response to anti-VEGF treatment, while patients with TT rs1061170 CFH genotype showed better functional and structural response to anti-VEGF agents. PMID: 29912491 Our analysis showed stronger contribution of ARMS2 in age-related macular degeneration (AMD) with reticular pseudodrusen (RPD) group versus AMD without RPD group, in comparison with CFH genotypes. PMID: 28593728 in Chinese lupus nephritis patients, the variants in the FH gene might affect the histopathologic subtypes and some clinical features of the disease PMID: 28403670 Study demonstrated that a novel complotype composed of CFB (rs4151667) in combination with CFB (rs641153) and CFH(rs800292) is strongly associated with complement activation and age-related macular degeneration status. PMID: 27241480 The rs193053835 single nucleotide polymorphism showed the most significant protective effect to be associated with susceptibility to Meningococcal disease. PMID: 27805046 Mapping rare, deleterious mutations in Factor H: Association with early onset, drusen burden, and lower antigenic levels in familial AMD. PMID: 27572114 AMD patients had significantly elevated nitrated CFH levels compared to controls (p = 0.0117). These findings strongly suggest that nitrated CFH contributes to AMD progression, and is a target for therapeutic intervention. PMID: 28159936 inhibition of the alternative pathway by factor H, with a concentration equivalent to a high physiological level, strongly reduced C5a levels and decreased proinflammatory cytokine production in human peripheral blood mononuclear cells. PMID: 27721145 Complement factor H Y402H (rs1061170) and age-related maculopathy susceptibility2 (ARMS2)/LOC387715 A69S (rs10490924) polymorphisms shown to have significant association with age-related macular degeneration (Meta-Analysis). PMID: 27269047 Regression analysis showed that ARMS2 TT genotype has a statistically significant effect on retinal angiomatous proliferation versus age-related macular degeneration compared to CFH genotypes (P < 0.001). PMID: 28005184 This study enclosed strong synergistic association of risk genotypes of C3 and CFH Y402H with AMD. We also revealed synergistic influence of CCL2-2518 and the at-risk genotype of the C3 in AMD with an estimated AP = 50.9% (adjusted AP = 24.7%). Present findings show that CCL2-2518 polymorphism is not an innocent bystander in AMD susceptibility when combined with the at-risk genotype of C3 (R102G). PMID: 28095095 Our results suggest that factor H can interfere with mycobacterial entry into macrophages and modulate inflammatory cytokine responses, particularly during the initial stages of infection, thus affecting the extracellular survival of the pathogen. PMID: 27262511 To our knowledge, this is the first evaluation of the involvement of the CFHR3/CFHR1 deletion and age-related macular degeneration in CFH Y402H polymorphism Brazilian patients. PMID: 26942649 The findings of the present study provide evidence that CFH gene variants and ARMS2/HTRA1 genes play a major role in the genetic susceptibility to AMD in a Greek population. These findings are of direct relevance for disease and help mapping the genetic chart of AMD. PMID: 26848857 Our results suggest the contribution of all four predicted CFH polymorphisms in age-related macular degeneration (AMD) susceptibility among the Iranian population. This association with CFH may lead to early detection and new strategies for prevention and treatment of AMD. PMID: 25612476 Development of polypoidal choroidal vasculopathy (PCV) in the unaffected fellow eye is associated with ARMS2 A69S genotype in patients with unilateral PCV. PMID: 26332911 Identification of rare CFH variant carriers may be important for upcoming complement-inhibiting therapies. Patients with an extensive drusen area, drusen with crystalline appearance, and drusen nasal to the optic disc are more likely to have a rare variant in the CFH gene. PMID: 28859202 C-reactive protein amino acids 35-47 mediate the interaction with complement factor H in lupus nephritis PMID: 28566480 OCT scans revealed lower retinal thickness in patients homozygous for CFH or ARMS2, which was caused by a significantly reduced photoreceptor layer. The number and ultrastructure of drusen were also significantly different. PMID: 28558370 VEGF inhibition decreases local CFH and other complement regulators in the eye and kidney through reduced VEGFR2/PKC-alpha/CREB signaling. PMID: 27918307 CFH rs1061170 has an important effect on age at onset of MDD in Han Chinese and may therefore be related to early pathogenesis of MDD. PMID: 26941266 Data suggest that disease-linked mutations in complement factor H (CFH) affect pivotal role of CFH in regulation of complement activation; mutations studied include those linked to atypical hemolytic uremic syndrome and age-related macular degeneration. PMID: 28637873 Factor I binds C3b-Factor H between Factor H domains 2 and 3 and a reoriented C3b C-terminal domain and docks onto the first scissile bond, while stabilizing its catalytic domain for proteolytic activity. PMID: 28671664 The VEGF haplotype TGA could be used as a marker for poor visual prognosis in Tunisian patients with neovascular AMD treated with bevacizumab. PMID: 27116510 Two protective, low-frequency, non-synonymous variants were significantly associated with a decrease in age-related macular degeneration (AMD)risk: A307V in PELI3 and N1050Y in CFH .We also identified a strong protective signal for a common variant (rs8056814) near CTRB1 associated with a decrease in AMD risk (logistic regression: OR = 0.71, P = 1.8 x 10-07). PMID: 28011711 this study shows that RNA interference of factor H in dendritic cells increased alloantigen-specific T-cell proliferation PMID: 28105653 monomeric CRP (mCRP) but not the pentameric form (pCRP) upregulates IL-8 and CCL2 levels in retinal pigment epithelial cells. Complement factor H (FH) binds mCRP to dampen its proinflammatory activity. FH from AMD patients carrying the "risk" His402 polymorphism displays impaired binding to mCRP. PMID: 26961257 The uromodulin-CFH interaction enhanced the cofactor activity of CFH for factor I-mediated cleavage of C3b to inactivated C3b. PMID: 27113631 Our results revealed that SNPs CD59-rs831626 and CFH-rs1065489 were associated with the susceptibility of acute anterior uveitis. PMID: 27419833 Our results show that age-related macular degeneration donors carrying the high risk allele for CFH (C) had significantly more mtDNA damage compared with donors having the wild-type genetic profile. PMID: 26854823 Data suggest that Staphylococcus aureus surface protein SdrE (serine-aspartate repeat protein E) functions as a 'clamp' to capture C-terminal tail of human CFH (complement factor H) at a specific ligand-binding site/groove via unique close-dock-lock-latch mechanism and thereby sequesters CFH on surface of S. aureus for complement evasion (immune evasion). PMID: 28258151 The haplotypic coinheritance of potentially functional variants (including missense variants, novel splice sites, and the CFHR3-CFHR1 deletion) was described for the four common haplotypes. Expression of the short and long CFH transcripts differed markedly between the retina and liver. PMID: 27196323 Data suggest that complement factor H (CFH) attaches to surface of host cells to inhibit complement activation and amplification, preventing destruction of the host cells; SdrE (serine-aspartate repeat protein) of Staphylococcus aureus binds to CFH allowing S. aureus to mimic a host cell and reducing bacterial killing by granulocytes. [Commentary] PMID: 28490660 Interaction effects between supplement groups and individual complement factor H (CFH) Y402H and age-related maculopathy susceptibility 2 (ARMS2) genotypes, and composite genetic risk groups combining the number of risk alleles for both loci, were evaluated for their association with progression PMID: 27471039 EMD were not AMD-independently associated with CFH or ARMS2 genotypes. Our results indicate that patients without AMD but with EMD can serve as controls in studies evaluating AMD risk factors. PMID: 26614632 Functional activities of FH are deficient in patients with ANCA-positive vasculitis. PMID: 27939215 role for serum FH levels in the host response to invasive pneumococcal infections PMID: 26802141 Despite limited power of this pilot study, our results suggest an association of HF with polymorphisms in ARMS2/HTRA1, CFH, APOE4/TOMM40, and VEGFA genes which could be triggered by modification of the extracellular matrix, altered complement system or lipid metabolism. PMID: 27552409 data suggest that R1210C is a unique C-terminal complement factor H mutation that behaves as a partial complement factor H deficiency, predisposing individuals to diverse pathologies with distinct underlying pathogenic mechanisms; the final disease outcome is then determined by R1210C-independent genetic risk factors PMID: 26376859 AMD progression rate is influenced by CFH, and suggest that variants within CFH may have different effects on risk versus progression. However, since CFH:rs10737680 was not significant after Bonferroni correction and explained only a relatively small portion of variation in progression rate beyond that explained by age PMID: 27832277 We describe a novel CFH/CFHR3 hybrid gene secondary to a de novo 6.3-kb deletion that arose through microhomology-mediated end joining rather than nonallelic homologous recombination. We confirmed a transcript from this hybrid gene and showed a secreted protein product that lacks the recognition domain of factor H and exhibits impaired cell surface complement regulation PMID: 26490391 The footprint of C3b on the FH surface matches existing crystal structures of C3b complexed with the N- and C-terminal fragments of FH. In addition, data revealed the position of the central portion of FH in the protein complex. Moreover, cross-linking studies confirmed the involvement of the C-terminus in the dimerization of FH. PMID: 27099340

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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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