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| Assay Time | |
| Detection Method | |
| Product Type | |
| Sample Type(s) | Blood, saliva, urine, agriculture etc |
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Overview
For quantitative determination of α-amylase enzyme activity. The assay uses OD585nm for signal readout. Compatible sample input includes Blood, saliva, urine, agriculture etc. Typical stated assay timing is 40 min.
Key elements and design rationale
- Readout format: OD585nm supports plate-based signal acquisition and consistent comparison across matched samples.
- Sample compatibility: The stated sample scope includes Blood, saliva, urine, agriculture etc, which is useful when aligning matrix type with calibration and control design.
- Analytical range context: The supplied specifications include a stated detection limit of 0.3 U/L for interpreting low-signal samples.
- Feature emphasis: Sensitive and accurate. Linear detection range 0.3 to 50 U/L α-amylase in 96-well plate assay.
Additional feature notes highlight Convenient. The procedure involves adding a single working reagent, incubation for 15 min, followed by the detection reagent and a 20-min incubation and reading the optical density at 585 nm. Available format information for this listing includes 100 Tests.
Biological background
This product is centered on measurement of α-amylase within the matrices described for the assay. In practice, datasets from this type of format are typically interpreted by comparing relative signal, activity, or abundance across matched control and experimental groups rather than relying on a single value in isolation. Careful alignment of sample matrix, incubation window, and calibration strategy is important when comparing results across plates, operators, or study days.
More details
AMYLASE belongs to the family of glycoside hydrolase enzymes that break down starch into glucose molecules by acting on α-1,4-glycosidic bonds. The α-amylases (EC 3.2.1.1) cleave at random locations on the starch chain, ultimately yielding maltotriose and maltose, glucose and “limit dextrin” from amylose and amylopectin. In mammals, α-amylase is a major digestive enzyme. Increased enzyme levels in humans are associated with salivary trauma, mumps due to inflammation of the salivary glands, pancreatitis and renal failure. Simple, direct and automation-ready procedures for measuring amylase activity are very desirable. BioAssay Systems’ EnzyChrom™ a-amylase assay method involves two steps: (1). α-amylase in the sample hydrolyzes starch and the product is rapidly converted to glucose by α-glucosidase and hydrogen peroxide by glucose oxidase; (2). hydrogen peroxide concentration is determined with a colorimetric reagent.
Detection method
Colorimetric (OD 585 nm).
Detection limit and analytical sensitivity
Reported detection limit: 0.3 U/L.
Procedures and timing
Stated procedure or timing information: 40 min.
Research relevance and current trends
- Plate-based quantification and side-by-side group comparison remain central use cases for this assay format.
- Short assay timing and plate compatibility support time-course or repeated-measure collection plans when handling is kept consistent.
- Matched standards, blanks, and replicate wells are typically used to improve interpretability across batches and sample matrices.
Common research applications
- Quantify α-amylase in blood, saliva, urine, agriculture by OD585 nm readout.
- Compare treatment or phenotype groups using matched blood, saliva, urine, agriculture handling.
- Monitor time-course or pre/post changes in blood, saliva, urine, agriculture across study conditions.
Interpretation is usually strongest when signal changes are assessed alongside matrix-matched controls, replicate agreement, and the assay's stated analytical window.
Notes for experimental interpretation
- Matrix composition, background signal, and sample handling can influence apparent response; compare like-with-like whenever possible.
- Use appropriate blanks, controls, and replicate wells to distinguish biological differences from plate, reagent, or handling variability.
Does glucose interfere with the assay?
The glucose content of the sample will add a significant background and I would recommend removing it from the sample:
– For samples known to contain glucose, use a membrane filter (e.g.
Microcon YM-10 from Millipore) to remove glucose: load 50 µL sample in a Microcon YM-10 (10 kDa cutoff) and add 500 µL Assay Buffer.
– Centrifuge at 14000 rpm for 30 min, check level of sample, ideally the sample level will be less than 50 µL. Add 500 µL Assay Buffer and repeat the centrifugation. Measure final sample volume with a pipetman and calculate dilution factor n = final sample volume/50 µL.
For laboratories requiring additional technical capacity, we provide scientific support services including assay execution, method guidance, product sourcing, and customization to align the assay with specific experimental objectives. If you need assistance selecting the appropriate kit configuration, adapting the workflow to your application, or identifying related research services, please click Talk to a Scientist, email support@biohippo.com, or review our Research Services; a member of our scientific team will follow up with recommendations tailored to your study.
The antioxidant and antidiabetic activity of the Arabian balsam tree Commiphora gileadensis in hyperlipidaemic male rats
El Rabey, H. A., et al. (2020). The antioxidant and antidiabetic activity of the Arabian balsam tree Commiphora gileadensis in hyperlipidaemic male rats. Journal of Taibah University for Science. 14(1): 831-841. Assay: Amylase in rat serum.
Novel bacterial surface display system based on the Escherichia coli protein mipa
Han, M. J. (2020). Novel bacterial surface display system based on the Escherichia coli protein mipa. Journal of Microbiology and Biotechnology. 30(7): 1097-1103. Assay: Amylase in Esherichia coli Surface Display System with B. subtilis.
Administration of encapsulated L-tryptophan improves duodenal starch digestion and increases gastrointestinal hormones secretions in beef cattle
Lee, S.-B., et al. (2020). Administration of encapsulated L-tryptophan improves duodenal starch digestion and increases gastrointestinal hormones secretions in beef cattle. Asian-Australasian Journal of Animal Sciences. 33(1): 91-99. Assay: Amylase in cattle duodenal fluid.
Protective effect of nypa fruticans wurmb
Bae, G.-S. (2020). Protective effect of nypa fruticans wurmb. Water extract on acute pancreatitis. Journal of Physiology & Pathology in Korean Medicine. 34(6): 334-340. Assay: Amylase in mouse serum.
Impacts of whey protein on starch digestion in rumen and small intestine of steers
Lee, Sang-Bum, et al (2019). Impacts of whey protein on starch digestion in rumen and small intestine of steers. Journal of Animal Science and Technology 61.2: 98-108. Assay: alpha-Amylase in beef steers duodenal fluid.
An efficient bacterial surface display system based on a novel outer membrane anchoring element from the Escherichia coli protein YiaT
Han, MJ & Lee SH (2015). An efficient bacterial surface display system based on a novel outer membrane anchoring element from the Escherichia coli protein YiaT. FEMS Microbiol. Lett. 362.1: 1-7. Assay: a-Amylase in Bacillus subtilis (bacteria) cells.
Han, MJ, and Seung HL (2015) An efficient bacterial surface display system based on a novel outer membrane anchoring ele
Han, MJ, and Seung HL (2015) An efficient bacterial surface display system based on a novel outer membrane anchoring element from the Escherichia coli protein YiaT.” FEMS Microbiology Letters 362.1: 1-7. Assay: alpha-Amylase in mammal cells.
Antioxidant Profile of Saliva among Young Men Using Mobile Phones
Abu Khadra, KM et al (2014). Antioxidant Profile of Saliva among Young Men Using Mobile Phones. Jordan Journal of Biological Sciences. 7(4):275-280. Assay: alpha-Amylase in human saliva.
Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats
Lee, KH et al (2014). Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats. J. Animal Sci. Techn. 56.1 : 6. Assay: a-Amylase in rat plasma.
Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats
Lee, KH et al (2014). Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats. Journal of Animal Science and Technology. 56:6. Assay: alpha-Amylase in sprague-dawley rats pancreas tissue.
Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats
Lee, KH et al.(2014). Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats. Journal of Animal Science and Technology 56.1: 6. Assay: alpha-Amylase in rat plasma.
Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats
Lee, Kyung-Hoon, et al.(2014). Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats.” Journal of Animal Science and Technology 56.1: 6. Assay: alpha-Amylase in mice plasma.
Age-related changes in salivary biomarkers
Mohannad N et al (2014). Age-related changes in salivary biomarkers. Journal of Dental Sciences. 9(1): 85-90. Assay: alpha-Amylase in human saliva.
Age-related changes in salivary biomarkers
Mohannad N et al (2014). Age-related changes in salivary biomarkers. Journal of Dental Sciences. 9(1): 85-90. Assay: a-Amylase in human Saliva.
Effect of Oral Administration of Intact Casein on Gastrointestinal Hormone Secretion and Pancreatic alpha-Amylase Activity in Korean Native Steer
Lee, SB et al (2013). Effect of Oral Administration of Intact Casein on Gastrointestinal Hormone Secretion and Pancreatic alpha-Amylase Activity in Korean Native Steer. Asian-Australasian Journal of Animal Sciences (AJAS). 26(5): 654-660. Assay: a-Amylase in steers (cow) pancreas (duodenal fluid).
Feeding barley grain steeped in lactic acid modulates rumen fermentation patterns and increases milk fat content in dairy cows
Iqbal S, et al (2009). Feeding barley grain steeped in lactic acid modulates rumen fermentation patterns and increases milk fat content in dairy cows. J Dairy Sci. 92(12):6023-32. Assay: alpha-Amylase in food grain.