HMGN3 Protein (AA 1-77) (His tag)
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- Target See all HMGN3 Proteins
- HMGN3 (High Mobility Group Nucleosomal Binding Domain 3 (HMGN3))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-77
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This HMGN3 protein is labelled with His tag.
- Application
- SDS-PAGE (SDS)
- Sequence
- MGSSHHHHHH SSGLVPRGSH MGSMPKRKSP ENTEGKDGSK VTKQEPTRRS ARLSAKPAPP KPEPKPRKTS AKKEPGAKIS RGAKGKKEEK QEAGKEGTEN
- Purity
- > 95 % by SDS - PAGE
- Top Product
- Discover our top product HMGN3 Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/mL
- Buffer
- Liquid. 20 mM Tris-HCl buffer ( pH 7.0) containing 10 % glycerol
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.
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- Target
- HMGN3 (High Mobility Group Nucleosomal Binding Domain 3 (HMGN3))
- Alternative Name
- HMGN3 (HMGN3 Products)
- Synonyms
- Trip7 Protein, PNAS-25 Protein, TRIP7 Protein, 1110002A15Rik Protein, 6330514M13Rik Protein, BB071015 Protein, high mobility group nucleosomal binding domain 3 L homeolog Protein, high mobility group nucleosomal binding domain 3 Protein, hmgn3.L Protein, HMGN3 Protein, Hmgn3 Protein
- Background
- HMGN3, also known as high mobility group nucleosomal binding domain 3, binds thyroid hormone receptor beta, but only in the presence of thyroid hormone. Thyroid hormone receptors are hormone-dependent transcription factors that regulate expression of a variety of specific target genes. It is thought to reduce the compactness of the chromatin fiber in nucleosomes, thereby enhancing transcription from chromatin templates. Recombinant human HMGN3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
- Molecular Weight
- 10.8 kDa(100aa) confirmed by MALDI-TOF
- NCBI Accession
- NP_620058
- UniProt
- Q15651
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