Analytical Data
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Gene name
RNASE7
- Application
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Alternative Names
RNASE7;Ribonuclease 7
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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
Q9H1E1
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Expression Region
29-156aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSKPKGMTS SQWFKIQHMQ PSPQACNSAM KNINKHTKRC KDLNTFLHEP FSSVAATCQT PKIACKNGDK NCHQSHGPVS LTMCKLTSGK YPNCRYKEKR QNKSYVVACK PPQKKDSQQF HLVPVHLDRV L
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Molecular Weight
17 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
RNASE7 is a member of the ribonuclease A (RNase A) superfamily and is known for its significant role in the innate immune response, particularly in the skin and respiratory tract. Discovered in keratinocytes and later found in various tissues, RNASE7 exhibits potent antimicrobial properties against a wide range of pathogens, including bacteria and viruses, by degrading their RNA. Its expression can be induced by pro-inflammatory cytokines, highlighting its importance in host defense mechanisms. Given its promising antimicrobial activity and potential therapeutic applications, researchers have focused on recombinant production of RNASE7 to study its structural and functional properties in greater detail. This includes characterizing its enzymatic activity, understanding its interactions with various microbial entities, and exploring its potential as a therapeutic agent for treating infections. Additionally, RNASE7's role as a signaling molecule in inflammation and cell proliferation has garnered interest, positioning it as a candidate for research in both immunology and molecular biology. As a result, recombinant RNASE7 has become an important subject of study, facilitating insights into its mechanisms of action and potential applications in medicine.
