RIZ1 Protein, Human
RIZ1 Protein, an S-adenosyl-L-methionine-dependent histone methyltransferase, specifically methylates 'Lys-9' of histone H3. Additionally, it acts as a DNA-binding transcription factor, showing affinity for the MTE within the HMOX1 gene. Implicated as a potential activator, RIZ1 suggests a regulatory role in HMOX1 gene expression beyond histone modification. RIZ1 Protein, Human is the recombinant human-derived RIZ1 protein, expressed by E. coli , with tag free.
- Species: Human
- Source: E. coli
Biological Activity
RIZ1 Protein, an S-adenosyl-L-methionine-dependent histone methyltransferase, specifically methylates 'Lys-9' of histone H3. Additionally, it acts as a DNA-binding transcription factor, showing affinity for the MTE within the HMOX1 gene. Implicated as a potential activator, RIZ1 suggests a regulatory role in HMOX1 gene expression beyond histone modification. RIZ1 Protein, Human is the recombinant human-derived RIZ1 protein, expressed by E. coli , with tag free.
RIZ1 protein serves as an S-adenosyl-L-methionine-dependent histone methyltransferase, demonstrating specificity in methylating 'Lys-9' of histone H3. Beyond its histone modification role, RIZ1 may also function as a DNA-binding transcription factor, with an affinity for the macrophage-specific TPA-responsive element (MTE) within the HMOX1 (heme oxygenase 1) gene. In this context, it is implicated as a potential transcriptional activator for HMOX1, suggesting a regulatory role in the expression of this gene.
Technical Parameters
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Species Human
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Source E. coli
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Tag Tag Free
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Accession
Q13029 (M1-A200)
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Molecular Construction
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N-term
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RIZ1 (M1-A200)
Accession # Q13029 -
C-term
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Protein Length
Partial
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Synonyms
PR domain zinc finger protein 2; MTB-ZF; Zinc finger protein RIZ; PRDM2; KMT8; RIZ
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AA Sequence
MNQNTTEPVAATETLAEVPEHVLRGLPEEVRLFPSAVDKTRIGVWATKPILKGKKFGPFVGDKKKRSQVKNNVYMWEVYYPNLGWMCIDATDPEKGNWLRYVNWACSGEEQNLFPLEINRAIYYKTLKPIAPGEELLVWYNGEDNPEIAAAIEEERASARSKRSSPKSRKGKKKSQENKNKGNKIQDIQLKTSEPDFTSA
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Predicted Molecular Mass
23 kDa
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Molecular Weight
Approximately 26 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Documentation
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)