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Mouse Anti-KMT2D Recombinant Antibody (2E1) (CBMAB-K1432-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
2E1
Antibody Isotype
IgG2a, κ
Application
ELISA, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a, κ
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
Concentration
0.5 mg/ml
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.

Target

Full Name
LYSINE METHYLTRANSFERASE 2D
Introduction
The protein encoded by this gene is a histone methyltransferase that methylates the Lys-4 position of histone H3. The encoded protein is part of a large protein complex called ASCOM, which has been shown to be a transcriptional regulator of the beta-globin and estrogen receptor genes. Mutations in this gene have been shown to be a cause of Kabuki syndrome. [provided by RefSeq, Oct 2010]
Entrez Gene ID
8085
UniProt ID
O14686
Alternative Names
Lysine Methyltransferase 2D; Myeloid/Lymphoid Or Mixed-Lineage Leukemia 2; Lysine (K)-Specific Methyltransferase 2D; Trinucleotide Repeat Containing 21; Lysine N-Methyltransferase 2D; ALL1-Related Protein; MLL2; MLL4; ALR; Myeloid/Lymphoid Or Mixed-Lineage Leukemia Protein 2; Histone-Lysine N-Methyltransferase MLL2;
Function
Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) (PubMed:25561738).
Part of chromatin remodeling machinery predominantly forms H3K4me1 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:25561738, PubMed:17500065).
Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription (PubMed:16603732).
Cellular Location
Nucleus
Involvement in disease
Kabuki syndrome 1 (KABUK1):
A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy.
More Infomation

Dhar, S. S., & Lee, M. G. (2021). Cancer-epigenetic function of the histone methyltransferase KMT2D and therapeutic opportunities for the treatment of KMT2D-deficient tumors. Oncotarget, 12(13), 1296.

Heward, J., Koniali, L., D’Avola, A., Close, K., Yeomans, A., Philpott, M., ... & Fitzgibbon, J. (2021). KDM5 inhibition offers a novel therapeutic strategy for the treatment of KMT2D mutant lymphomas. Blood, The Journal of the American Society of Hematology, 138(5), 370-381.

Alam, H., Tang, M., Maitituoheti, M., Dhar, S. S., Kumar, M., Han, C. Y., ... & Lee, M. G. (2020). KMT2D deficiency impairs super-enhancers to confer a glycolytic vulnerability in lung cancer. Cancer cell, 37(4), 599-617.

Wang, G., Chow, R. D., Zhu, L., Bai, Z., Ye, L., Zhang, F., ... & Chen, S. (2020). CRISPR-GEMM pooled mutagenic screening identifies KMT2D as a major modulator of immune checkpoint blockade. Cancer discovery, 10(12), 1912-1933.

Sun, P., Wu, T., Sun, X., Cui, Z., Zhang, H., Xia, Q., & Zhang, D. (2019). KMT2D inhibits the growth and metastasis of bladder Cancer cells by maintaining the tumor suppressor genes. Biomedicine & Pharmacotherapy, 115, 108924.

Fagan, R. J., & Dingwall, A. K. (2019). COMPASS Ascending: Emerging clues regarding the roles of MLL3/KMT2C and MLL2/KMT2D proteins in cancer. Cancer letters, 458, 56-65.

Li, S. S., Jiang, W. L., Xiao, W. Q., Li, K., Zhang, Y. F., Guo, X. Y., ... & Wan, R. (2019). KMT2D deficiency enhances the anti-cancer activity of L48H37 in pancreatic ductal adenocarcinoma. World Journal of Gastrointestinal Oncology, 11(8), 599.

Xiong, W., Deng, Z., Tang, Y., Deng, Z., & Li, M. (2018). Downregulation of KMT2D suppresses proliferation and induces apoptosis of gastric cancer. Biochemical and biophysical research communications, 504(1), 129-136.

Ardeshir-Larijani, F., Bhateja, P., Lipka, M. B., Sharma, N., Fu, P., & Dowlati, A. (2018). KMT2D mutation is associated with poor prognosis in non–small-cell lung cancer. Clinical lung cancer, 19(4), e489-e501.

Lv, S., Ji, L., Chen, B., Liu, S., Lei, C., Liu, X., ... & Lu, L. (2018). Histone methyltransferase KMT2D sustains prostate carcinogenesis and metastasis via epigenetically activating LIFR and KLF4. Oncogene, 37(10), 1354-1368.

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

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