Analytical Data
-
Gene name
clpP2
- Application
-
Alternative Names
clpP2；NCLPP7；ATP-dependent Clp protease proteolytic subunit 2. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O51698
-
Expression Region
1-198aa
-
AA Sequence
MTGKEDNDACVLHDKSLKLVLKSRSIVIAGEITKDVSRLFQEKILLLEAL DFKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTVGVGLVASAAALIF LAAKLENRFSLPFARYLLHQPLSGFKGVATDIEIYTNELNKVKKELNNII SKETGQKISKIEKDTDRDFWLDSSAAKKYGLVFEVVETKYQLEEFISA
-
Molecular Weight
27 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
CLP protease (caseinolytic protease) is a crucial ATP-dependent proteolytic complex found in various bacteria, including some pathogens. The CLP protease system plays a significant role in regulating protein turnover, maintaining cellular quality control, and facilitating stress responses. Among its subunits, CLP P2 is particularly interesting due to its involvement in substrate recognition and unfolding. Research on CLP P2 recombinant proteins has gained momentum as scientists seek to understand the molecular mechanisms underlying proteolytic activity and its implications in bacterial physiology and virulence. By studying the structure and function of CLP P2, researchers aim to explore its potential as a target for novel antibacterial therapies, especially in the face of increasing antibiotic resistance. Furthermore, recombinant CLP P2 can be utilized in various applications, including biotechnology and synthetic biology, for protein degradation and regulation. The generation of recombinant CLP P2 proteins opens avenues for dissecting the complex roles of the CLP protease system in cellular processes, thereby providing insights that are crucial for advancing our understanding of microbial life and developing innovative strategies to combat bacterial infections.
