Analytical Data
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Gene name
pep2
- Application
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Alternative Names
pep2；PEPP2；THG1；Rhox homeobox family member 2
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0QN14
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Expression Region
1-452aa
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AA Sequence
MTEPAKLPWS DWLPQQRWYA GRNRRLTGAE PSVIVGLRDD LDLVLVDADY ADGSRDRYQV LVCWDAAPVS EYSTVATIGA ADDRTGFDAL YDDEAPQFLL SLIDSSAVRS ASGAEVRFAK EPDAQLPLEA MAHVSDAEQS NTSVIFDRDA IFKVFRRVSS GINPDIELNR VLGRAGNPHV ARLLGTYEMA GADGTPETAW PLGMVTEFAA NAAEGWAMAT ASVRDLFAEG DLYAHEVGGD FAGESYRLGE AVASVHATLA ETLGTSQAAF PVDNVLARLS STAALVPELT EYAATIEERF AKLATETITV QRVHGDLHLG QVLRTPESWL LIDFEGEPGQ PLEERRAPDS PLRDVAGVLR SFEYAAYGPL VEQGSQNTDK QLAARAREWV ERNRTAFCDG YAAASGIDPR DSAPLLAAYE LDKAVYEAGY EARHRPGWLP IPLRSIARLT AA
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Molecular Weight
49.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
PEP2, or Protein Engineering and Production 2, is a recombinant protein that has garnered attention in the field of molecular biology due to its potential applications in various biotechnological and therapeutic contexts. The research surrounding PEP2 is driven by the need for innovative protein designs that can serve specific functions, including drug delivery systems, enzyme replacement therapies, and biosensors. Recombinant protein technology allows for the production of proteins with enhanced stability, specificity, and activity by manipulating the genetic code of organisms. PEP2, designed to exhibit improved performance characteristics, is often studied in the framework of its folding, solubility, and overall functional efficacy. The ongoing exploration of PEP2 seeks not only to optimize its production process but also to elucidate its interaction mechanisms within biological systems. By advancing our understanding of PEP2, researchers aim to exploit its properties to develop novel therapeutic strategies and improve existing techniques in protein engineering, thereby contributing to the broader domain of synthetic biology and personalized medicine.
