Analytical Data
-
Gene name
fpaP
- Application
-
Alternative Names
fpaP；CG005；PFAAP5；NEDD4-binding Protein 2-like 2
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O05420
-
Expression Region
1-289aa
-
AA Sequence
MIPITTPVGNFKVWTKRFGTNPKIKVLLLHGGPAMTHEYMECFETFFQREGFEFYEYDQLGSYYSDQPTDEKLWNIDRFVDEVEQVRKAIHADKENFYVLGNSWGGILAMEYALKYQQNLKGLIVANMMASAPEYVKYAEVLSKQMKPEVLAEVRAIEAKKDYANPRYTELLFPNYYAQHICRLKEWPDALNRSLKHVNSTVYTLMQGPSELGMSSDARLAKWDIKNRLHEIATPTLMIGARYDTMDPKAMEEQSKLVQKGRYLYCPNGSHLAMWDDQKVFMDGVIKFIKDVDTKSFN
-
Molecular Weight
41.6 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
FpaP, a member of the family of periplasmic-binding proteins, has garnered significant attention in recent years due to its potential applications in various biotechnological fields. Initially discovered in certain bacteria, FpaP is implicated in the transport of key nutrients, such as amino acids, across the periplasmic space, playing a vital role in bacterial metabolism and survival. The unique structural features of FpaP, characterized by a high-affinity ligand-binding domain and a flexible conformation, make it an ideal candidate for studies focused on protein engineering and biosensor development. Research has shown that recombinant FpaP can be produced in various expression systems, leading to insights into its functional mechanisms and interactions with ligands. Furthermore, understanding the biochemical properties of FpaP can facilitate the design of tailored enzymes for industrial applications, including drug delivery and environmental bioremediation. As the demand for sustainable solutions in various sectors grows, the exploration of FpaP's properties stands at the forefront of protein research, bridging gaps between fundamental science and practical applications.
