RBM4B Protein (AA 1-357) (Strep Tag)
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- Antigène Voir toutes RBM4B Protéines
- RBM4B (RNA Binding Motif Protein 4B (RBM4B))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-357
- Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette RBM4B protéine est marqué à la Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Séquence
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MVKLFIGNLP REATEQEIRS LFEQYGKVLE CDIIKNYGFV HIEDKTAAED AIRNLHHYKL HGVNINVEAS KNKSKASTKL HVGNISPTCT NQELRAKFEE YGPVIECDIV KDYAFVHMER AEDAVEAIRG LDNTEFQGKR MHVQLSTSRL RTAPGMGDQS GCYRCGKEGH WSKECPVDRT GRVADFTEQY NEQYGAVRTP YTMGYGESMY YNDAYGALDY YKRYRVRSYE AVAAAAAASA YNYAEQTMSH LPQVQSSAVP SHLNSTSVDP YDRHLLQNSG SAATSAAMAA AASSSYYGRD RSPLRRNAAV LPAVGEGYGY GPESEMSQAS AATRNSLYDM ARYEREQYVD RTRYSAF
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. - Attributs du produit
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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.
- Pureté
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- niveau d'endotoxine
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Classe de qualité
- Crystallography grade
- Top Product
- Discover our top product RBM4B Protéine
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- Indications d'application
- 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.
- Commentaires
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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.
- Conseil sur la manipulation
- Avoid repeated freeze-thaw cycles.
- Stock
- -80 °C
- Stockage commentaire
- Store at -80°C.
- Date de péremption
- Unlimited (if stored properly)
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- Antigène
- RBM4B (RNA Binding Motif Protein 4B (RBM4B))
- Autre désignation
- Rbm4b (RBM4B Produits)
- Synonymes
- RBM30 Protein, RBM4L Protein, ZCCHC15 Protein, ZCCHC21B Protein, ZCRB3B Protein, 4921506I22Rik Protein, AI504630 Protein, AI506404 Protein, Lark2 Protein, rbm4 Protein, rbm30 Protein, rbm4l Protein, zcrb3b Protein, zcchc15 Protein, MGC75893 Protein, RBM4B Protein, RNA binding motif protein 4B Protein, RNA binding motif protein 4B L homeolog Protein, RNA-binding protein 4B Protein, RBM4B Protein, Rbm4b Protein, rbm4b Protein, rbm4b.L Protein, LOC713553 Protein, LOC102180196 Protein, LOC100058729 Protein
- Sujet
- RNA-binding protein 4B (RNA-binding motif protein 30) (RNA-binding motif protein 4B) (RNA-binding protein 30),FUNCTION: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. {ECO:0000269|PubMed:17264215}.
- Poids moléculaire
- 40.0 kDa
- UniProt
- Q8VE92
- Pathways
- Photoperiodism
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