ATP6V1D Protein (AA 1-247) (Strep Tag)
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- Target Alle ATP6V1D Proteine anzeigen
- ATP6V1D (ATPase, H+ Transporting, Lysosomal 34kDa, V1 Subunit D (ATP6V1D))
- Protein-Typ
- Recombinant
- Proteineigenschaft
- AA 1-247
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Spezies
- Human
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Quelle
- Tobacco (Nicotiana tabacum)
- Aufreinigungstag / Konjugat
- Dieses ATP6V1D Protein ist gelabelt mit Strep Tag.
- Applikation
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequenz
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MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSEKDL EQRRAAGEVL EPANLLAEEK DEDLLFE
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)
- Güteklasse
- Crystallography grade
- Top Product
- Discover our top product ATP6V1D 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
- ATP6V1D (ATPase, H+ Transporting, Lysosomal 34kDa, V1 Subunit D (ATP6V1D))
- Andere Bezeichnung
- ATP6V1D (ATP6V1D Produkte)
- Synonyme
- ATP6M Protein, VATD Protein, VMA8 Protein, VHA36 Protein, 1110004P10Rik Protein, Atp6m Protein, Vma8 Protein, ATPase H+ transporting V1 subunit D Protein, ATPase, H+ transporting, lysosomal V1 subunit D Protein, H(+)-transporting V1 sector ATPase subunit D Protein, ATP6V1D Protein, Atp6v1d Protein, VMA8 Protein
- Hintergrund
- V-type proton ATPase subunit D (V-ATPase subunit D) (V-ATPase 28 kDa accessory protein) (Vacuolar proton pump subunit D),FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (PubMed:21844891). {ECO:0000250|UniProtKB:P39942, ECO:0000269|PubMed:21844891, ECO:0000269|PubMed:33065002}.
- Molekulargewicht
- 28.3 kDa
- UniProt
- Q9Y5K8
- Pathways
- Transition Metal Ion Homeostasis, Proton Transport
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