Zinc Finger Protein 110 (ZFP110) (AA 1-828) protein (Strep Tag)
Quick Overview for Zinc Finger Protein 110 (ZFP110) (AA 1-828) protein (Strep Tag) (ABIN3136885)
Target
Protein Type
Origin
Source
Application
Purity
Grade
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Protein Characteristics
- AA 1-828
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Purification tag / Conjugate
- Strep Tag
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Sequence
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MASTLPTTWP HESVKFEDVS LTFTEEEWAQ LDFQQKCLYR EIMMENYSNM ISVEHHFSKP NVISQLEKAE DCWPMQREIP QDTLPECSWP SPDPGMNSFP SKSPLMKIEV VEVLTLNKDV AGPRNALIQS LYPEDLNPGN LKPAQQPSKR LTDTEASRQK FRHFQYEESA GPQKAMSQLR KLCHQWLQPN TRSKKQILEL LVLEQFLNAL PEKFRVWVES QHPEDCKAVV ALLENMTSVS KDDASLACSS EATDQLKEKR KGVATLPVTF AAEVPAEEPV TFQDVAVDFN EEEWRLLGPT QKTEYHDVML ETLGNLVSVG WEPTLGNREL TPDSPIPVVK PIHDPNTNDL SRNGTQSTVF ESILEDGVKE MHSIESNQVG NLQEKGHPQK KFSESSKSQD QTSRHKSQGS LNEVLPRKYV KVKQKGTGKR KGRTNTISMT RGLRIRKQQK DSVEWQGRSG STPVTHGSSI KKQQQGSEQG KPGTSRDPIT LTVPAKVYQK ATGSEESIFM DSSDAMVPDV PPKIHQKGPE WHKVGESNNS MLQGSSVQNH QMESGAGRAS DNSLLTHALP VKSHQKGYKE GNVQGNRNSW KHIKPHQKGS KGERVEELST SEKHVPYVKN HLKTSERGKD REINASIKCD PYIKTYYRGS DVGRLRRANN CRKAFSLHAQ QISFIKIHKG SQVCRCSECG KLFRNARYFS VHKKIHTGER PYMCMACGKA FVQSSSLTQH LRIHSGERPF ECSECGRTFN DRSAISQHLR THTGAKPYHC ERCGKAFRQS SHLTRHERTH TGERPYVCIK CGKAFTQSSH LIGHQKTHGI KFKKQPKL
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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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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- Zinc Finger Protein 110 (ZFP110)
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Alternative Name
- Nrif1
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Background
- Neurotrophin receptor-interacting factor 1 (Neurotrophin receptor-interacting factor) (Zinc finger protein 110),FUNCTION: Transcription regulator involved in NGFR/p75(NTR)-mediated apoptosis. Essential component of the NGFR/p75(NTR) apoptotic pathway: upon ligand-binding and subsequent cleavage of NGFR/p75(NTR), binds to the intracellular domain (ICD) cleavage product of NGFR/p75(NTR), translocates to the nucleus and induces apoptosis, possibly by regulating expression of key regulators of apoptosis. Induces NGFR/p75(NTR)-mediated apoptosis in retina and sympathetic neurons. May also regulate expression of neuronal cholesterol biosynthesis genes. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression. {ECO:0000269|PubMed:10545116, ECO:0000269|PubMed:15668238, ECO:0000269|PubMed:16630834, ECO:0000269|PubMed:18677445, ECO:0000269|PubMed:18815271}.
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Molecular Weight
- 93.7 kDa
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UniProt
- Q923B3
Target
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