FAM48A/P38IP Protein (AA 1-530) (Strep Tag)
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- Target See all FAM48A/P38IP (SUPT20H) Proteins
- FAM48A/P38IP (SUPT20H) (Suppressor of Ty 20 Homolog (SUPT20H))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-530
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Origin
- Mouse
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Source
- Tobacco (Nicotiana tabacum)
- Purification tag / Conjugate
- This FAM48A/P38IP protein is labelled with Strep Tag.
- Application
- ELISA, SDS-PAGE (SDS), Western Blotting (WB)
- Sequence
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MQQAVEQALD CAEYIVESAQ QRPPKRKYLS SGRKSIFQKL YDLYVEECEK EPEVKKLRRN VNLLEKLVMQ ETLSCLVVNL YPGNEGYSLM LRGKNGSDSE TIRLPYEEGE LLEYLDAEEL PPILVDLLEK SQVNIFHCGC VIAEIRDYRQ SSNMKSPGYQ SRHILLRPTM QTLVCDVHSI TSDNHKWTQE DKLLLESQLI LATAEPLCLD PSVAVACTAN RLLYNRQKMN TRPMKRCWKR YSRSSLNRQQ DLSHGPPPPQ LRLLDFLQKR KERKAGQHYD LKISKAGNCV DMWKRSPCNL AVPSEVDVEK YAKVEESIKS DDSQPTMWPA HDVKDDYVFE CEGGNQYQKT KLTILQSLGD PLYYGKIQPW KADEENDSQM SPSHSSADDH SNWFVIGSKT DAERVVNQYQ ELVQNEAKCP VKMSHSSSGS AALSPGEEAE QAETSSIQSS VLGKGVKHRP PPIKLPSGSG NSSSGNYFTA QQASSFLKSP TPPPSCKPSL SRKSSVDLSQ VSMLSPAALS PASSSQRHES
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)
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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
- FAM48A/P38IP (SUPT20H) (Suppressor of Ty 20 Homolog (SUPT20H))
- Alternative Name
- Supt20h (SUPT20H Products)
- Synonyms
- SUPT20H Protein, AA667204 Protein, AI450544 Protein, D3Ertd300e Protein, Fam48a Protein, Supt20h Protein, p38IP Protein, RGD1307812 Protein, C13 Protein, C13orf19 Protein, FAM48A Protein, P38IP Protein, SPT20 Protein, bA421P11.4 Protein, SPT20 homolog, SAGA complex component Protein, suppressor of Ty 20 Protein, SUPT20H Protein, Supt20 Protein, Supt20h Protein
- Background
- Transcription factor SPT20 homolog (p38-interacting protein) (p38IP),FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) activation during gastrulation. Required for down-regulation of E-cadherin during gastrulation by regulating E-cadherin protein level downstream from NCK-interacting kinase (NIK) and independently of the regulation of transcription by FGF signaling and Snail. Required for starvation-induced ATG9A trafficking during autophagy. {ECO:0000269|PubMed:16751104}.
- Molecular Weight
- 59.5 kDa
- UniProt
- Q7TT00
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