TFIP11 Protein (AA 1-838) (Strep Tag)
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- Target See all TFIP11 Proteins
- TFIP11 (Tuftelin Interacting Protein 11 (TFIP11))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-838
- Origin
- Mouse
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Source
- Tobacco (Nicotiana tabacum)
- Purification tag / Conjugate
- This TFIP11 protein is labelled with Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequence
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MSLSHLYRDG EGHLDDDDDD ERENFEITDW DLQNEFNPNR QRHWQTKEEA TYGVWAERDS DEERPSFGGK RARDYSAPVN FISAGLKKGA AEEADSEDSD AEEKPVKQED FPKDLGPKKL KTGGNFKPSQ KGFSGGTKSF MDFGSWERHT KGIGQKLLQK MGYVPGRGLG KNAQGIINPI EAKQRKGKGA VGAYGSERTT QSLQDFPVAD SEEEAEEEFQ KELSQWRKDP SGSKKKPKYS YKTVEELKAK GRVSKKLTAP QKELSQVKVI DMTGREQKVY YSYSQISHKH SVPDEGVPLL AQLPPTAGKE ARMPGFALPE LEHNLQLLIE RTEQEIIQSD RQLQYERDMV VSLSHELEKT AEVLAHEERV ISNLSKVLAL VEECERRMQP HGADPLTLDE CARIFETLQD KYYEEYRLAD RADLAVAIVY PLVKDYFKDW HPLEDGSYGT QIISKWKSLL ENDQLLSHSS QDLSSDAFHR LMWEVWMPFV RNVVAQWQPR NCEPMVDFLD SWAHIIPVWI LDNILDQLIF PKLQKEVDNW NPLTDTVPIH SWIHPWLPLM QARLEPLYSP VRSKLSSALQ KWHPSDASAK LILQPWKEVL TPGSWEAFML RNIVPKLGMC LGELVINPHQ QHMDAFYWVM DWEGMISVSS LVGLLEKHFF PKWLQVLCSW LSNSPNYEEI TKWYLGWKSM FSDQVLAHPS VKDKFNEALD IMNRAVSSNV GAYMQPGARE NIAYLTHTER RKDFQYEAMQ ERREAENMAQ RGIGVAASSV PMNFKDLIET KAEEHNIVFM PVIGKRHEGK QLYTFGRIVI YIDRGVVFVQ GEKTWVPTSL QSLIDMAK
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us. - Characteristics
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Key Benefits:
- Made in Germany - from design to production - by highly experienced protein experts.
- Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
- These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.
The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
Expression System:- ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
- During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!
Concentration:- The concentration of our recombinant proteins is measured using the absorbance at 280nm.
- The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
- We use the Expasy's protparam tool to determine the absorption coefficient of each protein.
- Purification
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Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
- In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
- Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
- Purity
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- Endotoxin Level
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Top Product
- Discover our top product TFIP11 Protein
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- Application Notes
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
- Comment
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ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein! - Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- Unlimited (if stored properly)
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- Target
- TFIP11 (Tuftelin Interacting Protein 11 (TFIP11))
- Alternative Name
- Tfip11 (TFIP11 Products)
- Synonyms
- TFIP11 Protein, NTR1 Protein, Spp382 Protein, TIP39 Protein, bK445C9.6 Protein, hNtr1 Protein, 2810002G02Rik Protein, AF097181 Protein, AW046167 Protein, Srr1 Protein, TIP33 Protein, Tip39 Protein, STIP Protein, septin and tuftelin interacting protein Protein, tuftelin interacting protein 11 Protein, STIP Protein, TFIP11 Protein, Tfip11 Protein
- Background
- Tuftelin-interacting protein 11 (Septin and tuftelin-interacting protein 1) (STIP-1) (Tuftelin-interacting protein 39),FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix. {ECO:0000269|PubMed:15868102, ECO:0000269|PubMed:19857462}.
- Molecular Weight
- 96.3 kDa
- UniProt
- Q9ERA6
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