Analytical Data
-
Gene name
pepA
- Application
-
Alternative Names
Leucine aminopeptidase (EC:3.4.11.10) Short name: LAP Leucyl aminopeptidase
-
Species
Mycoplasma pneumoniae
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P75206
-
Expression Region
1-445aa
-
Molecular Weight
64.8 kDa
-
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
PepA, also known as aminopeptidase A, is an essential enzyme that plays a crucial role in protein metabolism by catalyzing the removal of amino acids from the N-terminus of peptide substrates. Its significance extends beyond basic metabolic functions; PepA is implicated in various biological processes, including antigen processing and the regulation of neuropeptide activity, making it a potential target for therapeutic interventions. Research has shown that PepA is involved in the pathophysiology of several diseases, including cancer and neurodegenerative disorders, as alterations in its activity can impact cellular functioning and protein homeostasis. Consequently, the investigation of PepA recombinant protein has garnered considerable attention within the scientific community. Techniques such as recombinant DNA technology enable the production of PepA in heterologous expression systems, facilitating the study of its enzymatic properties, structural biology, and potential as a drug target. Moreover, the availability of recombinant PepA allows for the development of specific inhibitors that could modulate its activity in pathological states. Understanding the structure-function relationship of PepA through studies involving its recombinant form could provide deeper insights into its role in various biochemical pathways and pave the way for innovative therapeutic strategies that leverage PepA modulation for disease treatment. This multifaceted research underscores PepA’s importance in both fundamental biochemistry and potential clinical applications, highlighting the need for continued exploration of its properties and functions.
