Analytical Data
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Gene name
SNIP1
- Application
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Alternative Names
SNIP1;Smad nuclear-interacting Protein 1
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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
Q8TAD8
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Expression Region
1-396aa
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AA Sequence
MKAVKSERER GSRRRHRDGD VVLPAGVVVK QERLSPEVAP PAHRRPDHSG GSPSPPTSEP ARSGHRGNRA RGVSRSPPKK KNKASGRRSK SPRSKRNRSP HHSTVKVKQE REDHPRRGRE DRQHREPSEQ EHRRARNSDR DRHRGHSHQR RTSNERPGSG QGQGRDRDTQ NLQAQEEERE FYNARRREHR QRNDVGGGGS ESQELVPRPG GNNKEKEVPA KEKPSFELSG ALLEDTNTFR GVVIKYSEPP EARIPKKRWR LYPFKNDEVL PVMYIHRQSA YLLGRHRRIA DIPIDHPSCS KQHAVFQYRL VEYTRADGTV GRRVKPYIID LGSGNGTFLN NKRIEPQRYY ELKEKDVLKF GFSSREYVLL HESSDTSEID RKDDEDEEEE EEVSDS
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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
SNIP1 (SIP1, SNIP1/2) is a member of the SNIP family of proteins known for their role in cellular processes such as signal transduction and transcriptional regulation. Research into SNIP1 has gained prominence due to its involvement in critical biological pathways, particularly those related to cell growth, differentiation, and apoptosis. Notably, SNIP1 has been implicated in various pathological conditions, including cancer, where its expression levels can influence tumor progression and response to therapy. The functional complexity of SNIP1, including its interactions with transcription factors and other signaling molecules, has attracted significant interest in the scientific community. Understanding the structural and functional properties of SNIP1, particularly through the study of its recombinant protein forms, is essential for elucidating its biological roles. Researchers aim to characterize SNIP1's interactions at the molecular level, analyze its impact on gene expression, and explore its potential as a therapeutic target. The generation of recombinant SNIP1 proteins allows for detailed biochemical studies, providing insights into the protein's mechanism of action and paving the way for potential applications in disease treatment and biotechnology. Overall, ongoing research on SNIP1 and its recombinant variants holds promise for advancing our understanding of cellular regulation and developing novel therapeutic strategies.
