SAR1A Protein (AA 1-198) (Strep Tag)
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- Antigène Voir toutes SAR1A Protéines
- SAR1A (SAR1 Homolog A (SAR1A))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-198
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Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette SAR1A protéine est marqué à la Strep Tag.
- Application
- ELISA, SDS-PAGE (SDS), Western Blotting (WB)
- Séquence
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MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLQMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLME SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI KGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID
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)
- Top Product
- Discover our top product SAR1A 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
- SAR1A (SAR1 Homolog A (SAR1A))
- Autre désignation
- Sar1a (SAR1A Produits)
- Synonymes
- T14P4.21 Protein, T14P4_21 Protein, DDBDRAFT_0203743 Protein, DDBDRAFT_0229965 Protein, DDB_0203743 Protein, DDB_0229965 Protein, sar1a Protein, LOC100283241 Protein, 1600019H17Rik Protein, Sara Protein, Sara1 Protein, SAR1 Protein, SARA1 Protein, masra2 Protein, Ras-related small GTP-binding family protein Protein, ARF/SAR superfamily protein Protein, SAR1 gene homolog A (S. cerevisiae) Protein, GTP-binding protein SAR1A Protein, secretion associated Ras related GTPase 1A Protein, secretion associated, Ras related GTPase 1A Protein, AT1G02620 Protein, sarA Protein, sar1a Protein, LOC100283241 Protein, Sar1a Protein, SAR1A Protein
- Sujet
- GTP-binding protein SAR1a,FUNCTION: Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES) (By similarity). {ECO:0000250}.
- Poids moléculaire
- 22.4 kDa
- UniProt
- P36536
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