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Merck
CN

SRP0315

JARID1A human

recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)

别名:

KDM5A, RBP2, lysine (K)-specific demethylase 5A

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关于此项目

NACRES:
NA.32
UNSPSC Code:
12352200
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产品名称

JARID1A human, recombinant, expressed in baculovirus infected Sf9 cells, ≥80% (SDS-PAGE)

biological 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)

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

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.

存储类别

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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分析证书(COA)

Lot/Batch Number

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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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