Analytical Data
-
Gene name
PRR5
- Application
-
Alternative Names
PRR5；PROTOR1；Proline-rich Protein 5
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P85299
-
Expression Region
1-388aa
-
AA Sequence
MRTLRRLKFM SSPSLSDLGK REPAAAADER GTQQRRACAN ATWNSIHNGV IAVFQRKGLP DQELFSLNEG VRQLLKTELG SFFTEYLQNQ LLTKGMVILR DKIRFYEGQK LLDSLAETWD FFFSDVLPML QAIFYPVQGK EPSVRQLALL HFRNAITLSV KLEDALARAH ARVPPAIVQM LLVLQGVHES RGVTEDYLRL ETLVQKVVSP YLGTYGLHSS EGPFTHSCIL EKRLLRRSRS GDVLAKNPVV RSKSYNTPLL NPVQEHEAEG AAAGGTSIRR HSVSEMTSCP EPQGFSDPPG QGPTGTFRSS PAPHSGPCPS RLYPTTQPPE QGLDPTRSSL PRSSPENLVD QILESVDSDS EGIFIDFGRG RGSGMSDLEG SGGRQSVV
-
Molecular Weight
42.7 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
PRR5 (proline-rich protein 5) is a member of the proline-rich protein family, which plays a crucial role in various biological processes, including cell signaling, growth, and differentiation. Recent studies have highlighted its involvement in cellular stress responses and its potential contributions to cancer progression and metastasis. Research has shown that PRR5 interacts with several signaling pathways, notably those related to the mammalian target of rapamycin (mTOR), which regulates cellular metabolism and growth. Given its unique structural features, such as multiple proline-rich domains, PRR5 is believed to mediate protein-protein interactions that are pivotal for cellular signaling networks. The recombinant expression of PRR5 allows for detailed functional analyses, enabling researchers to dissect its molecular mechanisms and explore its potential as a therapeutic target. The characterization of PRR5 through recombinant protein technology can facilitate the development of specific inhibitors or modulators that may be beneficial in treating diseases associated with aberrant signaling pathways, particularly in cancers. Thus, understanding PRR5's structure-function relationship through recombinant protein studies is essential for unveiling its biological roles and therapeutic potentials.
