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Mouse Anti-KDM5A Recombinant Antibody (EG1780) (CBMAB-EN2123-LY)

The product is antibody recognizes KDM5A. The antibody EG1780 immunoassay techniques such as: ELISA, WB.
See all KDM5A antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
EG1780
Antibody Isotype
IgG
Application
ELISA, WB

Basic Information

Immunogen
Recombinant fragment of Human KDM5A (C-terminus).
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Lysine Demethylase 5A
Introduction
This gene encodes a member of the Jumonji, AT-rich interactive domain 1 (JARID1) histone demethylase protein family. The encoded protein plays a role in gene regulation through the histone code by specifically demethylating lysine 4 of histone H3. The encoded protein interacts with many other proteins, including retinoblastoma protein, and is implicated in the transcriptional regulation of Hox genes and cytokines. This gene may play a role in tumor progression. [provided by RefSeq, Aug 2013]
Entrez Gene ID
5927
UniProt ID
P29375
Alternative Names
Lysine Demethylase 5A; Jumonji/ARID Domain-Containing Protein 1A; Lysine (K)-Specific Demethylase 5A; Retinoblastoma-Binding Protein 2; Histone Demethylase JARID1A; RBBP-2; RBBP2; RBP2; Jumonji, AT Rich Interactive Domain 1A (RBBP2-Like);
Function
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511).
May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464).
May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity).
Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228).
Biological Process
Chromatin remodelingManual Assertion Based On ExperimentIBA:GO_Central
Circadian regulation of gene expressionISS:UniProtKB
Histone H3-K4 demethylationManual Assertion Based On ExperimentIDA:CAFA
Negative regulation of histone deacetylase activityISS:UniProtKB
Negative regulation of transcription by RNA polymerase IIIEA:Ensembl
Positive regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of DNA-binding transcription factor activityManual Assertion Based On ExperimentIMP:CAFA
Cellular Location
Nucleus, nucleolus. Occupies promoters of genes involved in RNA metabolism and mitochondrial function.
Involvement in disease
A chromosomal aberration involving KDM5A has been found in M5 type acute myeloid leukemia. Translocation t(11;12)(p15;p13) with NUP98.
Chromosomal aberrations involving KDM5A have been found in M7 type childhood acute myeloid leukemia. Translocation t(11;12)(p15;p13) with NUP98

Xu, S., Wang, S., Xing, S., Yu, D., Rong, B., Gao, H., ... & Lan, F. (2021). KDM5A suppresses PML-RARα target gene expression and APL differentiation through repressing H3K4me2. Blood Advances, 5(17), 3241-3253.

Noort, S., Wander, P., Alonzo, T. A., Smith, J., Ries, R. E., Gerbing, R. B., ... & Meshinchi, S. (2021). The clinical and biological characteristics of NUP98-KDM5A pediatric acute myeloid leukemia. Haematologica, 106(2), 630.

Gaillard, S., Charasson, V., Ribeyre, C., Salifou, K., Pillaire, M. J., Hoffmann, J. S., ... & Vandromme, M. (2021). KDM5A and KDM5B histone-demethylases contribute to HU-induced replication stress response and tolerance. Biology Open, 10(5), bio057729.

Yang, G. J., Zhu, M. H., Lu, X. J., Liu, Y. J., Lu, J. F., Leung, C. H., ... & Chen, J. (2021). The emerging role of KDM5A in human cancer. Journal of hematology & oncology, 14(1), 1-18.

Yang, G. J., Wu, J., Miao, L., Zhu, M. H., Zhou, Q. J., Lu, X. J., ... & Chen, J. (2021). Pharmacological inhibition of KDM5A for cancer treatment. European Journal of Medicinal Chemistry, 226, 113855.

Kirtana, R., Manna, S., & Patra, S. K. (2020). Molecular mechanisms of KDM5A in cellular functions: Facets during development and disease. Experimental Cell Research, 396(2), 112314.

Wang, L., Gao, Y., Zhang, G., Li, D., Wang, Z., Zhang, J., ... & Liao, X. (2020). Enhancing KDM5A and TLR activity improves the response to immune checkpoint blockade. Science Translational Medicine, 12(560), eaax2282.

Yang, G. J., Ko, C. N., Zhong, H. J., Leung, C. H., & Ma, D. L. (2019). Structure-based discovery of a selective KDM5A inhibitor that exhibits anti-cancer activity via inducing cell cycle arrest and senescence in breast cancer cell lines. Cancers, 11(1), 92.

Mitsui, E., Yoshida, S., Shinoda, Y., Matsumori, Y., Tsujii, H., Tsuchida, M., ... & Mizukami, T. (2019). Identification of ryuvidine as a KDM5A inhibitor. Scientific Reports, 9(1), 9952.

Shokri, G., Doudi, S., Fathi-Roudsari, M., Kouhkan, F., & Sanati, M. H. (2018). Targeting histone demethylases KDM5A and KDM5B in AML cancer cells: a comparative view. Leukemia research, 68, 105-111.

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For research use only. Not intended for any clinical use.

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