Analytical Data
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Gene name
SNAI1
- Application
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Alternative Names
SNAI1;SNAH;Zinc finger Protein SNAI1
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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
O95863
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Expression Region
1-264aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPRSFLV RKPSDPNRKP NYSELQDSNP EFTFQQPYDQ AHLLAAIPPP EILNPTASLP MLIWDSVLAP QAQPIAWASL RLQESPRVAE LTSLSDEDSG KGSQPPSPPS PAPSSFSSTS VSSLEAEAYA AFPGLGQVPK QLAQLSEAKD LQARKAFNCK YCNKEYLSLG ALKMHIRSHT LPCVCGTCGK AFSRPWLLQG HVRTHTGEKP FSCPHCSRAF ADRSNLRAHL QTHSDVKKYQ CQACARTFSR MSLLHKHQES GCSGCPR
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Molecular Weight
32 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
SNAI1 (Snail Family Transcriptional Repressor 1) is a crucial transcription factor that plays a significant role in embryonic development and epithelial-mesenchymal transition (EMT), a process essential for tissue remodeling, wound healing, and cancer metastasis. The overexpression of SNAI1 has been implicated in various aggressive cancers, as it enhances the migratory and invasive properties of tumor cells by promoting EMT. Given its pivotal role in these biological processes, the study of SNAI1 recombinant protein has gained considerable attention. Researchers are particularly interested in characterizing its structure-function relationships, understanding its interaction with other proteins, and elucidating its regulatory mechanisms. The development of SNAI1 recombinant proteins allows for the investigation of its biological activities in vitro and in vivo, facilitating the exploration of potential therapeutic targets in cancer treatment. Moreover, these proteins serve as valuable tools for studying the molecular pathways involved in EMT and cellular differentiation. As such, research surrounding SNAI1 recombinant proteins not only enhances our understanding of fundamental biological processes but also opens avenues for innovative cancer therapies.
