Anti-Factor H antibody [OX-24] (Biotin) (ab112197)


  • Product nameAnti-Factor H antibody [OX-24] (Biotin)
    See all Factor H primary antibodies
  • Description
    Mouse monoclonal [OX-24] to Factor H (Biotin)
  • ConjugationBiotin
  • Specificityab112197 recognizes the Human serum complement protein factor H and a 43- 49kD truncated form of factor H present at low levels (1-5ug/ml) in plasma and urine.
  • Tested applicationsSuitable for: ELISAmore details
  • Species reactivity
    Reacts with: Human, Non Human Primates
    Does not react with: Sheep, Rabbit, Chicken, Cow, Pig
  • Immunogen

    Human complement Factor H.


  • FormLiquid
  • Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
  • Storage bufferPreservative: 0.02% Sodium azide
    Constituents: 99% PBS, 0.5% BSA
  • Concentration information loading...
  • ClonalityMonoclonal
  • Clone numberOX-24
  • MyelomaNS0
  • IsotypeIgG1
  • Research areas


Our Abpromise guarantee covers the use of ab112197 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
ELISA 1/500. Plates were coated with 2 ug/ml purified Factor H, and HRPO streptavidin was used for detection.


  • FunctionFactor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
  • Tissue specificityExpressed by the liver and secreted in plasma.
  • Involvement in diseaseGenetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:126700]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss.
    Defects in CFH are the cause of complement factor H deficiency (CFH deficiency) [MIM:609814]. CFH deficiency determines uncontrolled activation of the alternative complement pathway with consumption of C3 and often other terminal complement components. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome. CFH deficiency patients may show increased susceptibility to meningococcal infections.
    Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:235400]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.
    Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:610698]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
  • Sequence similaritiesContains 20 Sushi (CCP/SCR) domains.
  • Cellular localizationSecreted.
  • Information by UniProt
  • Database links
  • Alternative names
    • adrenomedullin binding protein antibody
    • age related maculopathy susceptibility 1 antibody
    • AHUS 1 antibody
    • AHUS1 antibody
    • AMBP 1 antibody
    • AMBP1 antibody
    • ARMD 4 antibody
    • ARMD4 antibody
    • ARMS 1 antibody
    • ARMS1 antibody
    • beta 1 H globulin antibody
    • beta 1H antibody
    • beta1H antibody
    • CFAH_HUMAN antibody
    • CFH antibody
    • CFHL 3 antibody
    • CFHL3 antibody
    • Complement factor H antibody
    • complement factor H, isoform b antibody
    • Factor H antibody
    • factor H like 1 antibody
    • FH antibody
    • FHL 1 antibody
    • FHL1 antibody
    • H factor 1 (complement) antibody
    • H factor 1 antibody
    • H factor 2 (complement) antibody
    • HF 1 antibody
    • HF 2 antibody
    • HF antibody
    • HF1 antibody
    • HF2 antibody
    • HUS antibody
    • MGC88246 antibody
    see all

References for Anti-Factor H antibody [OX-24] (Biotin) (ab112197)

This product has been referenced in:
  • Alsenz J  et al. Structural and functional analysis of the complement component factor H with the use of different enzymes and monoclonal antibodies to factor H. Biochem J 232:841-50 (1985). Read more (PubMed: 2936333) »
  • Sim E  et al. Monoclonal antibodies against the complement control protein factor H (beta 1 H). Biosci Rep 3:1119-31 (1983). Read more (PubMed: 6199050) »

See all 2 Publications for this product

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Both antibodies are derived from the same clone, OX-24. Not only is one conjugated, the buffer components are slightly different as well. However, even if clones do sometimes show different behaviour regarding reactivi...

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Of the Factor H antibodies we carry, only the OX23 and the OX24 clones appear to have epitope mapping data. The following two papers describe the clones. Both clones apparently recognize an N-terminal 38 kDa regi...

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