Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: >= 75% SDS-PAGE
- Active: Yes
- Tags: DDDDK tag N-Terminus, Avi tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant human KDM5B / PLU1 / Jarid1B protein (Active)
See all KDM5B / PLU1 / Jarid1B proteins and peptides
Biological activitySpecific Activity: 0.11 pmol/min/µg.
Purity>= 75 % SDS-PAGE.
Expression systemBaculovirus infected Sf9 cells
Protein lengthFull length protein
Predicted molecular weight179 kDa
Amino acids2 to 1544
TagsDDDDK tag N-Terminus , Avi tag N-Terminus
Our Abpromise guarantee covers the use of ab271567 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.63% Tris HCl, 0.64% Sodium chloride, 0.02% Potassium chloride, 0.04% Tween, 20% Glycerol (glycerin, glycerine), 0.01% TCEP
80 µg/ml DDDDK peptide
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Cancer/testis antigen 31
- Histone demethylase JARID1B
FunctionHistone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.
Tissue specificityUbiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level).
Sequence similaritiesBelongs to the JARID1 histone demethylase family.
Contains 1 ARID domain.
Contains 1 JmjC domain.
Contains 1 JmjN domain.
Contains 3 PHD-type zinc fingers.
DomainBoth the JmjC domain and the JmjN domain are required for enzymatic activity.
The 2 first PHD-type zinc finger domains are required for transcription repression activity.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab271567 has not yet been referenced specifically in any publications.