ImmunoCAP Allergen Components
Providing a Clear Clinical Picture

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Our goal is to provide broad test menus with clinically relevant whole allergens and allergen components to help clinicians diagnose allergy and prepare a more comprehensive management plan. We offer the broadest menu of more than 100 quantitative allergen component tests, ranging from foods and inhalants to occupational allergens and more, measuring specific IgE antibodies to individual proteins.

During the last decade, we have launched more than 40 new allergen component tests, including cutting edge, clinically relevant components such as alpha-gal, Can f 5 (male-dog specific), and Ara h 2 (from peanut), among others. Phadia™ Laboratory Systems offer the capability to set up automated reflex-testing of relevant allergen components based on positivity of the whole allergen test(s). Most of our tests are based on recombinantly produced allergen components, which offer a high degree of purity and consistency. The majority of evidence gathered for allergen component testing is based on ImmunoCAP™ tests.1

More detailed answers enabling personalized care

With ImmunoCAP Allergen Component testing along with clinical history, a detailed sensitization profile can be obtained, helping healthcare providers to:

  • Differentiate between species-specific allergy and cross-reactivity.2,3
  • Assess the risk for systemic reactions.2,3
  • Identify relevant allergens for successful immunotherapy.2,3

A detailed sensitization profile can help answer many clinically relevant questions, such as:2,3

  • Can the patient tolerate baked egg or milk?
  • Is the patient with a positive peanut test result at increased risk for systemic reactions, or only mild symptoms?
  • Is it the dog, cat, or both causing the symptoms?
  • Can a female dog be tolerated?
  • Is the bee, wasp, or both species of insects causing the anaphylactic shock?
  • Is immunotherapy suitable or not; and to what allergen?

ImmunoCAP Allergen Components – The peanut example

Including ImmunoCAP Peanut Allergen Components in the diagnostic workup enables clinicians to determine sensitization on a protein level. With this information the clinicians can be helped to make a more refined diagnosis, asses the risk for a systemic reaction and consequently prepare a more comprehensive management plan.2,3


Peanut proteins and assessment of risk for systemic reaction

f 13
  • High levels of peanut IgE can predict the likelihood of peanut sensitivity, but may not be soley predictive of reactions or allergic response4
  • LOWEST RISK of systemic reaction5
  • Highly cross-reactive with pollen, plant food and venoms5
Bet v2
  • LOWEST RISK of systemic reaction5,6
  • Cross-reactive with pollens5
Ara h 8
f 352
  • LOWEST RISK of systemic reaction7,8
  • Risk of mild, localized symptoms, such as itching/tingling of the lips, mouth, and oropharynx9
  • Cross-reactive with pollens (e.g., birch)9
Ara h 9
f 427
  • VARIABLE RISK of systemic reaction including anaphylaxis10,11
  • Often accompanied by sensitization to other peanut proteins12
  • Cross-reactive with fruits with pits (e.g., peaches)7
Ara h 1, 2, 3, 6
f 422, f 423, f424, f447
  • HIGHER RISK of systemic reaction including anaphylaxis7,13
  • Sensitization to Ara h 2 is nearly always associated with clinical peanut allergy14
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1.       Data on File. Thermo Fisher Scientific. July 2017.

2.       Canonica, G.W., et al., A WAO - ARIA - GA(2)LEN consensus document on molecular-based allergy diagnostics. World Allergy Organ J, 2013. 6(1): p. 17.

3.       Matricardi, P.M., et al., EAACI Molecular Allergology User's Guide. Pediatr Allergy Immunol, 2016. 27 Suppl 23: p. 1-250.

4.       Nicolaou N, Poorafshar M, Murray C, et al. Allergy or tolerance in children sensitized to peanut: prevalence and differentiation using component-resolved diagnostics. J Allergy Clin Immunol. 2010;125(1):191-197.

5.       Bradshaw N, A Clinical Reference Guide to Molecular Allergy. Go Molecular! Molecular Allergy –The Basics, 2014.

6.       Katelaris CH: Food allergy and oral allergy or pollen-food syndrome. Curr Opin Allergy Clin Immunol 2010, 10:246–251.

7.       Asarnoj A, Nilsson C, Lidholm J, et al. Peanut component Ara h 8 sensitization and tolerance to peanut. J Allergy Clin Immunol. 2012;130(2):468-472.

8.       Nucera E, et al. Hypersensitivity to major panallergens in a population of 120 patients. Postepy Dermatol Alergol. 2015 Aug; 32(4): 255–261.

9.       Mittag D, Akkerdaas J, Ballmer-Weber BK, et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol. 2004;114(6):1410-1417.

10.    Lauer I, Dueringer N, Pokoj S, et al. The nonspecific lipid transfer protein, Ara h 9, is an important allergen in peanut. Clin Exp Allergy. 2009;39(9):1427-1437.

11.    Sastre J: Molecular diagnosis in allergy. Clin Exp Allergy 2010, 40:1442–1460.

12.   Movérare R, Ahlstedt S, Bengtsson U, et al. Evaluation of IgE antibodies to recombinant peanut allergens in patients with reported reactions to peanut. Int Arch Allergy Immunol. 2011;156(3):282-290.

13.    Peeters KA, Koppelman SJ, van Hoffen E, et al. Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy. 2007;37(1):108-115.

14.    Asarnoj A, Movérare R, Östblom E, et al. IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds. Allergy. 2010;65(9):1189-1195.