Ara h 6.0101

Food

Product Code Quantity Product Name Downloads Data Sheet
52500
52501
0.1 mg
1.0 mg

Ara h 1.0101

Ara h 1.0101 is a seed storage protein from Arachis hypogaea (peanut) found in the cotyledon. It is a heat stable 7S vicilin-like globulin with a stable trimeric form that comprises 12 to 16% of the total protein in peanut extracts. The protein is one of the main storage proteins of the seed and therefore of high necessity during plant development.
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50100
50101
0.1 mg
1.0 mg

Ara h 2.0201

Ara h 2 consists of two isoforms, called Ara h 2.0101 and Ara h 2.0201. The second isoform contains other IgE epitopes and has similar but higher IgE binding than Ara h 2.0101 (81% vs. 77%) . Ara h 2.0201, generally known as the most important peanut allergen, is a conglutin storage protein and accounts together with Ara h 6.0101 for the majority of the IgE immune response.
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52600
52601
0.1 mg
1.0 mg

Ara h 3.0101

Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are considered to be isoforms.
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51900
51901
0.1 mg
1.0 mg

Ara h 6.0101

Ara h 6.0101 is a conglutin, belonging to the 2S albumin protein family. Together with Ara h 2.0201, it is considered one of the most potent elicitors of anaphylaxis. Both proteins contain multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure.
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52700
52701
0.1 mg
1.0 mg

Ara h 8.0101

Ara h 8.0101 is a Bet v 1-homologous panallergen, belonging to the PR-10 protein family. It is cross-reactive with Bet v 1 from silver birch and Gly m 4 from soy bean. The minor allergen has low stability to roasting and no stability to gastric digestion and is thought to be responsible for oral allergy syndrome.
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52000
52001
0.1 mg
1.0 mg

Ara h 9.0101

The lipid transfer protein (LTP) Ara h 9 is a small molecule with high resistance to digestion and heat denaturation. Several different LTPs have been identified as relevant allergens in plant foods and pollens and are often associated with severe reactions in addition to oral allergy syndrome.
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53700
53701
0.1 mg
1.0 mg

Bos d 5 (β-Lactoglobulin; non recombinant)

β-Lactoglobulin is a heat-labile protein resistant to acid hydrolysis and known as one of the best characterized lipid-binding proteins. It has been shown that over 90% of the cow milk allergic patients show presence of Bos d 5 (β-lactoglobulin) specific IgE antibodies.
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53800
53801
0.1 mg
1.0 mg

Bos d 6 (Serum albumin; non recombinant)

Bovine serum albumin (Bos d 6) occurs as a minor allergen in cow's milk. Its main role is the transport, metabolism and distribution of ligands and the protection from free radicals. More than 90% of cow milk allergic patient samples show IgE binding to this allergen.
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53900
53901
0.1 mg
1.0 mg

Bos d 8 (Casein; non recombinant)

Casein (Bos d 8) is thermo- and digestion- stable, makes up about 75-80% of all Milk protein and occurs also in cheese and dairy products. It consists of proteins ranging from 19 to 25 kDa. Up to 63 % of milk-allergic children show IgE binding to Bos d 8 in enzyme immunoassay.
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54000
54001
0.1 mg
1.0 mg

Bos d Lactoferrin (non recombinant)

Lactoferrin (Bos d lactoferrin) is a major allergen and present in the whey fraction of milk. It can be found in most species at levels below 1%. This iron-binding glycoprotein of the transferrin family has antimicrobial activity and is therefore used as disinfectant substance in food industry.
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51800
51801
0.1 mg
1.0 mg

Cor a 1.0401

Cor a 1.0401 represents the major hazelnut allergen from Corylus avellana. This pathogenesis-related protein, PR-10, belongs to the family of Bet v 1 homologues and is closely related to the major hazel pollen allergen Cor a 1.0103.

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53200
53201
0.1 mg
1.0 mg

Gal d 1 (Ovomucoid; non recombinant)

Of the individuals suffering from food allergy, approx. 31% of the children and approx. 8% of the adults are allergic to egg. Ovomucoid, Gal d 1, represents up to 11% of the egg white protein content. The heat-stable trypsin inhibitor is the immunodominant protein fraction in egg white.
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53300
53301
0.1 mg
1.0 mg

Gal d 2 (Ovalbumin; non recombinant)

With approx. 54% Gal d 2 is the most abundant egg white protein. It has been used most extensively in research as model allergen. The heat-labile phosphoglycoprotein is an inactive member of the serine protease inhibitor superfamily (serpins) and is used as an additive in a number of vaccines.
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53400
53401
0.1 mg
1.0 mg

Gal d 3 (Conalbumin; non recombinant)

Ovotransferrin, Gal d 3, also known as conalbumin (up to 13 % of egg white), has a strong iron-binding capability and thus can be used as an antioxidant, antimicrobial or iron-supplementing agent, in food and particularly infant food.
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50500
50401
0.1 mg
1.0 mg

Gly m 4.0101

Glycine max (Gly m) 4.0101 is a soybean protein whose expression is induced under stress conditions like starvation giving rise to its alternative name starvation-associated message 22 (SAM 22) or stress-induced protein SAM22. It is a homologue of Betula verrucosa (Bet v) 1, a major birch pollen allergen.
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50600
50601
0.1 mg
1.0 mg

Gly m 5.0101

Upon germination, the Glycine max seed storage protein Gly m 5.0101 serves as carbon and nitrogen source for the developing seedling. This protein is also known as beta-conglycinin and belongs to the superfamily of 7 S globulins, also known as 7 S vicilins.

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52800
52801
0.1 mg
1.0 mg

Mal d 1.0108

Major apple (Malus domestica) allergen Mal d 1, a ribonuclease, is a heat-sensitive allergen and belongs to the protein class of pathogenesis-related (PR) proteins. The allergen shares homologous IgE epitopes with major birch pollen allergen Bet v 1 and Cor a 1 from hazelnut pollen.

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54100
54101
0.1 mg
1.0 mg

Pen a 1.0101

Pen a 1.0101, a Tropomyosin, is the only major allergen in brown shrimp Penaeus aztecus. The panallergen is a highly conserved and soluble muscle protein characterized by an alpha-helical homodimeric, coiled-coil structure.

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