NUDT16 Protein (AA 1-195) (Strep Tag)

Catalog No. ABIN3135744

Product Details

Target: NUDT16 (Nudix (Nucleoside Diphosphate Linked Moiety X)-Type Motif 16 (NUDT16))

Protein Type: Recombinant

Protein Characteristics: AA 1-195

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This NUDT16 protein is labelled with Strep Tag.

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

Sequence: MEGHRKVELS EALALGPDWR HACHALLYAP DPRKLFGRIP MRFAVLMQMR FDGRLGFPGG FVDAQDSCLE DGLNRELREE LGEAMSAFRV ERSDYRSSHI AARPRVVAHF YAKRLTLEQL QAVEARAPQA KDHGLEVLGL VRVPLYVLRD GEGGLPAFLE NSFIGAAREQ LLEALQDLKL LDPGIIAKLK IPDSK
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.

Characteristics: 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: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. 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.
2. 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.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

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. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: NUDT16 (Nudix (Nucleoside Diphosphate Linked Moiety X)-Type Motif 16 (NUDT16))

Alternative Name: Nudt16 (NUDT16 Products)

Synonyms: RGD1311387 Protein, 2310041H06Rik Protein, 2810047L04Rik Protein, 2900006H04Rik Protein, AI851783 Protein, x29 Protein, nudix hydrolase 16 Protein, nudix (nucleoside diphosphate linked moiety X)-type motif 16 Protein, nudix hydrolase 16 L homeolog Protein, Nudt16 Protein, NUDT16 Protein, nudt16.L Protein

Background: U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase),FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA, metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (By similarity). Acts also as a phosphatase, hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (PubMed:32432673). {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:20081199, ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:32432673}.

Molecular Weight: 21.8 kDa

UniProt: Q6P3D0

Pathways: Positive Regulation of Response to DNA Damage Stimulus