Analytical Data
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Gene name
RNPEP
- Application
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Alternative Names
RNPEP；APB；Aminopeptidase B
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Species
Human
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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
Q9H4A4
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Expression Region
1-650aa
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AA Sequence
MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPP GPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGS EEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGV CWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDG FTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVW AEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGM ENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGF TMYAQRRISTILFGAAYTCLEAATGRALLRQHMDITGEENPLNKLRVKIE PGVDPDDTYNETPYEKGFCFVSYLAHLVGDQDQFDSFLKAYVHEFKFRSI LADDFLDFYLEYFPELKKKRVDIIPGFEFDRWLNTPGWPPYLPDLSPGDS LMKPAEELAQLWAAEELDMKAIEAVAISPWKTYQLVYFLDKILQKSPLPP GNVKKLGDTYPSISNARNAELRLRWGQIVLKNDHQEDFWKVKEFLHNQGK QKYTLPLYHAMMGGSEVAQTLAKETFASTASQLHSNVVNYVQQIVAPKGS
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Molecular Weight
99 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
The research on RNPEP recombinant proteins has gained attention due to the significance of RNPEP (Arginine-N-glycyl Peptidase) in various physiological and pathological processes. RNPEP is an intracellular protease involved in the cleavage of arginine-glycine-rich peptides, playing a crucial role in protein homeostasis, cell signaling, and immune responses. Alterations in RNPEP activity have been implicated in several diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. Understanding the structure and function of RNPEP can provide insights into its biological roles and potential therapeutic applications. The development of recombinant RNPEP proteins allows researchers to study the enzyme's mechanisms, substrate specificity, and interactions with other cellular proteins in a controlled environment. This knowledge is essential for exploring RNPEP as a target for drug development and for designing inhibitors that could modulate its activity in disease contexts. Additionally, the ability to produce these proteins in sufficient quantities opens avenues for further functional assays and structural studies, paving the way for advancing our understanding of RNPEP's contributions to health and disease.
