Literature summary for 3.1.1.32 extracted from

Seismann, H.; Blank, S.; Cifuentes, L.; Braren, I.; Bredehorst, R.; Grunwald, T.; Ollert, M.; Spillner, E.
Recombinant phospholipase A1 (Ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity (2010), Clin. Mol. Allergy, 8, 7-7.

Search for more literature for 3.1.1.32

Application

Application	Comment	Organism
medicine	may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy. Recombinant Ves v 1 is an essential component to assess the sensitisation of individuals to yellow jacket venom and its recombinant availability complemented with Ves v 5 and phospholipase A2 from honeybee venom (Api m 1) allows for clear assignment of sensitisation patterns	Vespula vulgaris

Cloned(Commentary)

Cloned (Comment)	Organism
PCR product subcloned into the pAcGP67-B baculovirus transfer vector, expressed as wild-type and enzymatically inactivated mutant in Sf9-insect cells	Vespula vulgaris

Protein Variants

Protein Variants	Comment	Organism
S137G/N165A	lacks phospholipase activity	Vespula vulgaris

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
37000	-	x * 37000, recombinant enzyme, SDS-PAGE	Vespula vulgaris

Organism

Organism	UniProt	Comment	Textmining
Vespula vulgaris	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by nickel-chelating affinity chromatography	Vespula vulgaris

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Vespula vulgaris	-

Subunits

Subunits	Comment	Organism
?	x * 37000, recombinant enzyme, SDS-PAGE	Vespula vulgaris

Synonyms

Synonyms	Comment	Organism
phospholipase A1	-	Vespula vulgaris
Ves v 1	-	Vespula vulgaris

General Information

General Information	Comment	Organism
physiological function	is capable for activation of human basophils, relevance of Ves v 1 in hymenoptera venom allergy	Vespula vulgaris

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Release 2023.1 (January 2023)