Analytical Data
-
Gene name
PPIAL4A
- Application
-
Alternative Names
PPIAL4A；COAS2；PPIAL4B；Peptidyl-prolyl cis-trans isomerase A-like 4A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y536
-
Expression Region
1-164aa
-
AA Sequence
MVNSVVFFDITVDGKPLGRISIKLFADKILKTAENFRALSTGEKGFRYKGSCFHRIIPGFMCQGGDFTRHNGTGDKSIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICAAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITIADCGQF
-
Molecular Weight
34.2 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
PPIAL4A, or Peptidyl-Prolyl Isomerase A4, is a member of the cyclophilin family of proteins, which are known for their ability to catalyze the isomerization of proline residues in polypeptides. This enzymatic activity has significant implications for protein folding, stability, and function, and PPIAL4A has been implicated in various biological processes, including cell signaling, immune response, and regulation of gene expression. Recent studies have highlighted the potential role of PPIAL4A in various diseases, particularly cancer, where it may influence tumor progression and drug resistance. The interest in PPIAL4A as a target for therapeutic intervention has spurred research into its structural characteristics, interactions with other proteins, and the mechanisms underlying its biological functions. Understanding the significance of PPIAL4A through the development of recombinant proteins enables scientists to explore its activity in detail, including screening potential inhibitors or modulators that could pave the way for novel cancer treatments. Thus, the recombinant production of PPIAL4A not only facilitates in vitro studies to elucidate its role in cellular pathways but also holds promise for the identification of new strategies for disease management and therapeutic development.
