Every item is shipped based on the best shipping method assessed for the temperature requirements of that specific item. Items are grouped and shipped together whenever
possible, and a separate shipping charge will be included for each shipping method required. Shipping charges listed below are from our US warehouses to the Contiguous US,
Alaska, Hawaii, Canada and Puerto Rico. Shipping charges for countries outside the US and Canada will be determined once order has been received
Please note: We can not ship to PO boxes
Express Blue Ice
Express Dry Ice
Animal Health Prescription Item
SHIPPING METHODS & CHARGES
Ships via FedEx Ground to Contiguous US, Alaska, Canada, Monday through Friday. This method is used for less temperature sensitive items such as lab ware and animal
health products, bulky and/or heavy items
Labware ships FedEx Ground free of charge to the contiguous US
The formation of stable highly organized protein aggegrates, known as amyloid fibrils, is associated with several debilitating human diseases, including Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jakob disease (1,2). In each of these conditions, a peptide or protein that is normally soluble accumulates into insoluble fibrils (1,2). Muscle acylphosphatase (AcP) has emerged as a significant model system to study protein misfolding and aggregation (1,3-6). It is particularly suitable for these studies because muscle AcP is a small, simple protein of only 98 amino acids consisting of a five-stranded antiparallel b-sheet and two parallel a-helices. Mutations in the muscle AcP between residues 16-31 and 87-98, which includes its phosphate binding site at Arg-23, significantly increases the rate of aggregation (1,6). These mutations correlate with changes in the hydrophobicity of AcP and a conversion of the a-helical structures to b-sheets. Therefore, a reduction in the net charge of a protein may be a key determinant in some forms of protein deposition diseases.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.