Analytical Data
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Gene name
pepP
- Application
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Alternative Names
pepP；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
P15034
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Expression Region
2-441aa
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AA Sequence
SEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL TASVVKKPEE IEALMVAARK Q
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Molecular Weight
49.8 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
Related Products
Protein Description
PepP, or peptidase P, is an important enzyme that plays a crucial role in various biological processes, including protein metabolism and regulation. Studying pepP recombinant proteins is vital for several reasons. First, the elucidation of its structure and function can provide insights into the enzymatic mechanisms of peptide cleavage, which is fundamental for understanding protein turnover and amino acid availability in cells. Furthermore, investigating pepP has implications in medicine, particularly in the context of various diseases where peptide regulation is disrupted, such as cancer and metabolic disorders. Recombinant techniques allow for the production of large quantities of pure pepP proteins, facilitating detailed biochemical assays, structural analyses, and potential therapeutic applications. Moreover, the alignment of pepP from various organisms aids in the comparative study of evolutionary adaptations in peptide metabolism. The production of recombinant pepP can also support the development of inhibitors or modulators that could serve as valuable tools in both research and therapeutic settings. Overall, the study of pepP recombinant proteins is a multidisciplinary endeavor that bridges biochemistry, molecular biology, and pharmacology, with the potential to advance our understanding of fundamental biological processes and to drive innovations in disease treatment.
