ACAA2 Protein (AA 1-397) (Strep Tag)
Quick Overview for ACAA2 Protein (AA 1-397) (Strep Tag) (ABIN3074034)
Target
See all ACAA2 ProteinsProtein Type
Origin
Source
Application
Purity
Grade
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Protein Characteristics
- AA 1-397
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Purification tag / Conjugate
- This ACAA2 protein is labelled with Strep Tag.
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Sequence
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MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET VDSVIMGNVL QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV NGCQEICVKE AEVVLCGGTE SMSQAPYCVR NVRFGTKLGS DIKLEDSLWV SLTDQHVQLP MAMTAENLAV KHKISREECD KYALQSQQRW KAANDAGYFN DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK KDGTVTAGNA SGVADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If 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 in one-step affinity chromatography
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.
The big advantage of ordering our predefined custom 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 against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
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Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
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Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System Wheat germConjugate GST tagOrigin HumanPrice $488.72Expression System Escherichia coli (E. coli)Conjugate His-IF2DI TagOrigin HumanPrice $604.62Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $676.92Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $593.56Expression System Escherichia coli (E. coli)ConjugateOrigin HumanPrice $1,387.43Expression System HEK-293 CellsConjugate Myc-DYKDDDDK TagOrigin HumanPrice $1,112.40Expression System BacteriaConjugate His tagOrigin HumanPrice $520.52Your project requires further customization? Contact us and discover our custom protein solutions
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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.
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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
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Buffer
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The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein. -
Handling Advice
- Avoid repeated freeze-thaw cycles.
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Storage
- -80 °C
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Storage Comment
- Store at -80°C.
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Expiry Date
- 12 months
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- ACAA2 (Acetyl-CoA Acyltransferase 2 (ACAA2))
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Alternative Name
- ACAA2
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Background
- 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) (Acetyl-CoA acetyltransferase) (EC 2.3.1.9) (Acetyl-CoA acyltransferase) (Acyl-CoA hydrolase, mitochondrial) (EC 3.1.2.-, EC 3.1.2.1, EC 3.1.2.2) (Beta-ketothiolase) (Mitochondrial 3-oxoacyl-CoA thiolase) (T1),FUNCTION: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (Probable). Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies (Probable). Also displays hydrolase activity on various fatty acyl-CoAs (PubMed:25478839). Thereby, could be responsible for the production of acetate in a side reaction to beta-oxidation (Probable). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (PubMed:18371312). {ECO:0000269|PubMed:18371312, ECO:0000269|PubMed:25478839, ECO:0000305|PubMed:25478839}.
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Molecular Weight
- 41.9 kDa
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UniProt
- P42765
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Pathways
- Monocarboxylic Acid Catabolic Process
Target
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