Analytical Data
-
Gene name
ACP5
- Application
-
Alternative Names
TRAP; TrATPase; Tartrate Resistant Acid Phosphatase; Type 5 acid phosphatase
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P13686
-
Expression Region
Gln79~Arg318
-
Molecular Weight
57kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ACP5, also known as Acidic Calcium Phosphate Phosphatase 5, is a key enzyme involved in bone mineralization and phosphate metabolism. Its primary role is to hydrolyze inorganic pyrophosphate (PPi) to inorganic phosphate (Pi), which is essential for the proper mineralization of bone and teeth. Dysregulation of ACP5 activity can lead to pathological conditions such as osteomalacia and deficiencies in bone density, highlighting its significance in skeletal health. Recent studies have focused on the structure-function relationship of ACP5, utilizing recombinant protein techniques to produce and characterize the enzyme in vitro. This allows researchers to explore its catalytic mechanisms and regulatory pathways, providing insights into its role in bone physiology and potential therapeutic targets for bone-related diseases. Furthermore, understanding ACP5's interaction with other biomolecules and its regulation by post-translational modifications is crucial for elucidating its broader implications in metabolic disorders. The development of specific inhibitors or enhancers of ACP5 could pave the way for novel strategies in treating conditions associated with abnormal phosphate metabolism, illustrating the need for continued research in this area.
