SRP0315
JARID1A human
recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)
Synonyme(s) :
KDM5A, RBP2, lysine (K)-specific demethylase 5A
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A propos de cet article
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
aqueous solution
Assay:
≥80% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
Mol wt:
125 kDa
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Laissez-nous vous aiderbiological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
125 kDa
packaging
pkg of 20 μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... KDM5A(5927)
General description
Human JARID1A, also known as KDM5A and RBBP2, (GenBank Accession No. NM_001042603), amino acids 1-1090 with C-terminal FLAG-tag, MW= 125 kDa, expressed in Sf9 cells via a Baculovirus expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Classe de stockage
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Laura J C M van Zutven et al.
Genes, chromosomes & cancer, 45(5), 437-446 (2006-01-19)
Chromosome rearrangements are found in many acute leukemias. As a result, genes at the breakpoints can be disrupted, forming fusion genes. One of the genes involved in several chromosome aberrations in hematological malignancies is NUP98 (11p15). As NUP98 is close
Xue Zhou et al.
Cancer research, 70(10), 4214-4221 (2010-04-22)
Histone H3 lysine 4 (H3K4) trimethylation (H3K4me3) at the promoter region of genes has been linked to transcriptional activation. In the present study, we found that hypoxia (1% oxygen) increased H3K4me3 in both normal human bronchial epithelial Beas-2B cells and
Alexander Roesch et al.
Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, 18(9), 1249-1257 (2005-04-02)
In malignant melanomas, the loss of cell cycle control is thought to be due to a lack of retinoblastoma protein (pRb)-activity. Members of the previously described family of retinoblastoma-binding proteins (RBPs) are supposed to act as pRb-modulating factors. Based on
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