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Complement factor H/CFH Protein, Human, Recombinant (His)

Catalog No. TMPK-00790

Factor H is the major soluble inhibitor of complement, where its binding to self markers (i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of self by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e., non-self) and cancer cells (i.e., altered-self) can hijack factor H to evade the immune response.

Complement factor H/CFH Protein, Human, Recombinant (His)

Complement factor H/CFH Protein, Human, Recombinant (His)

Catalog No. TMPK-00790
Factor H is the major soluble inhibitor of complement, where its binding to self markers (i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of self by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e., non-self) and cancer cells (i.e., altered-self) can hijack factor H to evade the immune response.
Pack SizePriceAvailabilityQuantity
100 μg$4187-10 days
500 μg$1,6707-10 days
1 mg$2,8007-10 days
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Product Information

Biological Activity
Immobilized Human Factor H, His Tag at 0.2μg/ml (100μl/well) on the plate. Dose response curve for Anti-Factor H Antibody, hFc Tag with the EC50 of 14.8ng/ml determined by ELISA.
Description
Factor H is the major soluble inhibitor of complement, where its binding to self markers (i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of self by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e., non-self) and cancer cells (i.e., altered-self) can hijack factor H to evade the immune response.
Species
Human
Expression System
HEK293 Cells
TagC-His
Accession NumberP08603-1
Synonyms
HUS,HF2,HF1,HF,H factor 1,FHL1,FH,Complement factor H,CFHL3,CFH,ARMS1,ARMD4,AMBP1,AHUS1
Construction
Ser860-Arg1231
Protein Purity
> 95% as determined by Tris-Bis PAGE; > 95% as determined by HPLC
Molecular Weight42.8 kDa (predicted). Due to glycosylation, the protein migrates to 60-68 kDa based on Tris-Bis PAGE result.
Endotoxin< 1 EU/μg by the LAL method.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing PBS (pH 7.4). Typically, 8% trehalose is incorporated as a protective agent before lyophilization.
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice.
Research Background
Factor H is the major soluble inhibitor of complement, where its binding to self markers (i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of self by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e., non-self) and cancer cells (i.e., altered-self) can hijack factor H to evade the immune response.

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