LAP3 Protein (AA 1-519) (Strep Tag)
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- Target Alle LAP3 Proteine anzeigen
- LAP3 (Cytosol Aminopeptidase (LAP3))
- Protein-Typ
- Recombinant
- Proteineigenschaft
- AA 1-519
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Spezies
- Maus
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Quelle
- Tobacco (Nicotiana tabacum)
- Aufreinigungstag / Konjugat
- Dieses LAP3 Protein ist gelabelt mit Strep Tag.
- Applikation
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequenz
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MYLLPLPAAA RVALRRLGVR GLWDRGLSTA DMTKGLVLGI YAKDKDDDLP QFTSAGESFN KLVSGKLREM LNISGPPLKA GKTRTFYGLH QDFPSVVVVG LGKRSAGVDD QENWHEGKEN IRAAVAAGCR QVQDLELPSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK VAVSAKLHGS GDLEAWEKGV LFASGQNLAR HLMESPANEM TPTRFAEIIE KNLKSASSKT KVHIRPKSWI EEQEMGSFLS VAKGSEEPPV FLEIHYMGSP NATEAPLVFV GKGITFDSGG ISIKASANMD LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE ASVETGDRVW RMPLFEHYTR QVIDCQLADV NNLGKYRSAG ACTAAAFLRE FVTHTKWAHL DIAGVMTNKD EIPYLRKGMS GRPTRTLIEF LLRFSKDSS
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. - Produktmerkmale
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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.
- Aufreinigung
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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.
- Reinheit
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- Endotoxin-Niveau
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Top Product
- Discover our top product LAP3 Protein
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- Applikationshinweise
- 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.
- Kommentare
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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! - Beschränkungen
- Nur für Forschungszwecke einsetzbar
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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.
- Handhabung
- Avoid repeated freeze-thaw cycles.
- Lagerung
- -80 °C
- Informationen zur Lagerung
- Store at -80°C.
- Haltbarkeit
- Unlimited (if stored properly)
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- Target
- LAP3 (Cytosol Aminopeptidase (LAP3))
- Andere Bezeichnung
- Lap3 (LAP3 Produkte)
- Synonyme
- LAP Protein, LAPEP Protein, PEPS Protein, 2410015L10Rik Protein, AA410100 Protein, LAP-3 Protein, Lap Protein, Lapep Protein, Pep-7 Protein, Pep-S Protein, Pep7 Protein, Peps Protein, cytosol aminopeptidase Protein, leucine aminopeptidase 3 Protein, pepA Protein, Plabr_1567 Protein, Dester_0800 Protein, Weevi_0186 Protein, Marky_0570 Protein, Halhy_2623 Protein, FsymDg_3217 Protein, Flexsi_2186 Protein, Runsl_3980 Protein, lap3 Protein, LAP3 Protein, Lap3 Protein
- Hintergrund
- Cytosol aminopeptidase (EC 3.4.11.1) (Cysteinylglycine-S-conjugate dipeptidase) (EC 3.4.13.23) (Leucine aminopeptidase 3) (LAP-3) (Leucyl aminopeptidase) (Peptidase S) (Proline aminopeptidase) (EC 3.4.11.5) (Prolyl aminopeptidase),FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status. {ECO:0000250|UniProtKB:P00727}.
- Molekulargewicht
- 56.1 kDa
- UniProt
- Q9CPY7
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