Dairy proteins are widely considered the benchmark for high-quality dietary protein, owing to their balanced amino acid (AA) composition, high digestibility, and substantial essential amino acid (EAA) content(1). Recent years have seen a rise in consumer demand for protein resulting in the “proteinification” of the food environment. The dairy industry in New Zealand produces large quantities of proteins that are utilised as ingredients in a wide range of consumer products globally, while these products all originate from raw milk, they differ in their AA profiles as they are fractionated into different product streams to optimise their functionality for a variety of applications. Previously, the data pool for the AA content of various dairy powders was limited with unverified accuracy. This study addresses some of these gaps in the data and explains the variation in AA profiles between a variety of dairy powders. AA content was determined by high performance liquid chromatography. Products examined included whole milk powder (WMP), skim milk powder (SMP), cheese whey protein concentrate (WPC-C), lactic acid casein whey protein concentrate (WPC-L), high-fat whey protein concentrate (WPC-HF), hydrolysed whey protein concentrate (WPH), whey protein isolate (WPI), and demineralised whey protein (D90). The AA content for WMP and SMP were different between 12 of the 18 AAs measured (p < 0.05), attributed to milk fat globular membrane proteins present in the WMP samples. WPC-C and WPC-L comparison indicated higher levels of threonine (MD (95% C.I.) = 22.92 (21.96, 23.88); p<0.001), serine (MD (95% C.I.) = 9.33 (8.41, 10.24); p<0.001), glutamic acid (MD (95% C.I.) = 11.73 (9.58, 13.88); p<0.001), and proline (MD (95% C.I.) = 18.27 (17.29, 19.24); p<0.001) in WPC-C but lower levels of tyrosine (MD (95% C.I.) = -3.67 (-4.24, -3.09); p<0.001), phenylalanine (MD (95% C.I.) = −3.71 (-4.22, -3.20); p<0.001), and tryptophan (MD (95% C.I.) = -4.74 (-5.30, -4.18); p<0.001), attributed to the different methods of separation from casein proteins. WPI and WPC-HF varied in all AAs except histidine (MD (95% C.I.) = -0.33 (-0.75, 0.09); p=0.113) due to minor protein components. D90 and WPC-C demonstrated significant differences (p<0.05) in all but three AAs, Proline (MD (95% C.I.) = -1.63 (-6.28, 3.02); p=0.467), Tyrosine (MD (95% C.I.) = -3.39 (-7.00, 0.22); p=0.064) and Arginine (MD (95% C.I.) = -1.19 (-2.61, 0.24); p=0.096) due to filtering and demineralisation processes. Protein sources originating from the same raw material can end up with significantly different AA profiles due to fractionation and extraction processes. Understanding that these differences exist increases awareness of the need to formulate protein rich foods based on total protein and AA content to ensure the key benefits of protein are being delivered to the consumer.