ATP6V1C2 Protein (AA 1-427) (Strep Tag)

Catalog No. ABIN3075282

This Recombinant ATP6V1C2 protein is produced in Cell-free protein synthesis (CFPS).

Quick Overview for ATP6V1C2 Protein (AA 1-427) (Strep Tag) (ABIN3075282)

Target: ATP6V1C2 (ATPase, H+ Transporting, Lysosomal 42kDa, V1 Subunit C2 (ATP6V1C2))

Protein Type: Recombinant

Origin: Human

Source: Cell-free protein synthesis (CFPS)

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Purity: approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Product Details

Protein Characteristics: AA 1-427

Purification tag / Conjugate: This ATP6V1C2 protein is labelled with Strep Tag.

Sequence: MSEFWLISAP GDKENLQALE RMNTVTSKSN LSYNTKFAIP DFKVGTLDSL VGLSDELGKL DTFAESLIRR MAQSVVEVME DSKGKVQEHL LANGVDLTSF VTHFEWDMAK YPVKQPLVSV VDTIAKQLAQ IEMDLKSRTA AYNTLKTNLE NLEKKSMGNL FTRTLSDIVS KEDFVLDSEY LVTLLVIVPK PNYSQWQKTY ESLSDMVVPR STKLITEDKE GGLFTVTLFR KVIEDFKTKA KENKFTVREF YYDEKEIERE REEMARLLSD KKQQYQTSCV ALKKGSSTFP DHKVKVTPLG NPDRPAAGQT DRERESEGEG EGPLLRWLKV NFSEAFIAWI HIKALRVFVE SVLRYGLPVN FQAVLLQPHK KSSTKRLREV LNSVFRHLDE VAATSILDAS VEIPGLQLNN QDYFPYVYFH IDLSLLD
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: 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.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).

Application Details

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.

Comment:

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

Handling

Format: Liquid

Buffer: 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.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: ATP6V1C2 (ATPase, H+ Transporting, Lysosomal 42kDa, V1 Subunit C2 (ATP6V1C2))

Alternative Name: ATP6V1C2

Background: V-type proton ATPase subunit C 2 (V-ATPase subunit C 2) (Vacuolar proton pump subunit C 2),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 (By similarity). 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). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity). {ECO:0000250|UniProtKB:P21282, ECO:0000250|UniProtKB:P21283, ECO:0000250|UniProtKB:P31412}.

Molecular Weight: 48.8 kDa

UniProt: Q8NEY4

Pathways: Transition Metal Ion Homeostasis, Proton Transport