Insects have been consumed by people for millennia and have recently been proposed as a complementary, sustainable source of protein to feed the world’s growing population. The development of insects for food requires technology to explore their allergenic potential. Insects and crustaceans both belong to the arthropod family. Crustacean (shellfish) allergies are both relatively common and potentially severe; hence, the cross-reactivity of the immune system with insect proteins (e.g. tropomyosin and arginine kinase) is a potential health concern. In this study, LC-MS/MS was used to explore the proteome of whole, roasted whole and roasted powdered cricket products. Eight protein extraction protocols that encompass different buffer compositions, including one with a pre-extraction defatting step, were compared using the total number of protein and distinct peptide identifications as a qualitative measure. Within this data, 20 putative cross-reactive shellfish allergens were identified, of which three were arginine kinase (AK) proteoforms. Subsequently, a multiple reaction monitoring MS assay was developed for the AK proteoforms and applied to the five extraction methods that yielded the highest number of protein identifications. The urea/thiourea buffer was shown to maximally extract AKs from cricket samples, while the abundance of AKs was noted to vary between different cricket extracts. This targeted assay demonstrated that allergen abundance/ detectability varies according to the different food processing approaches.