Rabbit Anti-KDM5A Recombinant Antibody (CBLY1-068) (CBMAB-K0695-LY)

Name: Rabbit Anti-KDM5A Recombinant Antibody (CBLY1-068)
SKU: CBMAB-K0695-LY
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

CBLY1-068

Application

WB, FC

Specificity

Mouse, Rat, 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

Purity

> 95% Purity determined by SDS-PAGE.

Storage

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

More Infomation

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

Human	5927
Mouse	214899
Rat	312678

UniProt ID

Human	P29375
Mouse	Q3UXZ9
Rat	E9PSW7

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
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For research use only. Not intended for any clinical use.

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