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Mouse Anti-MLLT1 (AA 472-559) Recombinant Antibody (CBFYM-2299) (CBMAB-M2484-FY)

This product is mouse antibody that recognizes MLLT1. The antibody CBFYM-2299 can be used for immunoassay techniques such as: ELISA, IF, WB.
See all MLLT1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2299
Antibody Isotype
IgG2a, k
Application
ELISA, IF, WB

Basic Information

Immunogen
Recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: GRRSPESCSK PEKILKKGTY DKAYTDELVE LHRRLMALRE RNVLQQIVNL IEETGHFNVT NTTFDFDLFS LDETTVRKLQ SCLEAVA
Specificity
Human
Antibody Isotype
IgG2a, k
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 freeze/thaw cycles.
Epitope
AA 472-559

Target

Full Name
MLLT1, Super Elongation Complex Subunit
Introduction
MLLT1 is a Protein Coding gene. Diseases associated with MLLT1 include Borderline Leprosy and Indeterminate Leprosy. Among its related pathways are Gene Expression and Formation of HIV elongation complex in the absence of HIV Tat. An important paralog of this gene is MLLT3.
Entrez Gene ID
4298
UniProt ID
Q03111
Alternative Names
MLLT1, Super Elongation Complex Subunit; Myeloid/Lymphoid Or Mixed-Lineage Leukemia; Translocated To, 1; YEATS Domain-Containing Protein 1; YEATS1; LTG19; ENL; Myeloid/Lymphoid Or Mixed-Lineage Leukemia (Trithorax Homolog, Drosophila); Translocated To, 1
Function
Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948).

Specifically recognizes and binds acetylated and crotonylated histones, with a preference for histones that are crotonylated (PubMed:27105114).

Has a slightly higher affinity for binding histone H3 crotonylated at 'Lys-27' (H3K27cr) than 'Lys-20' (H3K9cr20) (PubMed:27105114).

Acts as a key chromatin reader in acute myeloid leukemia by recognizing and binding to acetylated histones via its YEATS domain, thereby regulating oncogenic gene transcription.
Biological Process
Chromatin remodeling Source: GO_Central
Histone acetylation Source: GO_Central
Negative regulation of protein kinase activity Source: Ensembl
Regulation of transcription by RNA polymerase II Source: GO_Central
Cellular Location
Nucleus
Involvement in disease
A chromosomal aberration involving MLLT1 is associated with acute leukemias. Translocation t(11;19)(q23;p13.3) with KMT2A/MLL1. The result is a rogue activator protein.

Raux, B., Buchan, K. A., Bennett, J., Christott, T., Dowling, M. S., Farnie, G., ... & Londregan, A. T. (2024). Discovery of PFI-6, a small-molecule chemical probe for the YEATS domain of MLLT1 and MLLT3. Bioorganic & Medicinal Chemistry Letters, 98, 129546.

Tan, L., Wang, L., Liu, J., & Yu, Y. (2023). Circvrk1 downregulation attenuates brain microvascular endothelial cell damage induced by oxygen–glucose deprivation through modulating the miR-150-5p/MLLT1 axis. Experimental Brain Research, 241(3), 781-791.

Yu, N., Tian, W., Liu, C., Zhang, P., Zhao, Y., Nan, C., ... & Liu, Y. (2023). miR-122-5p Promotes Peripheral and Central Nervous System Inflammation in a Mouse Model of Intracerebral Hemorrhage via Disruption of the MLLT1/PI3K/AKT Signaling. Neurochemical Research, 48(12), 3665-3682.

Kabra, A., & Bushweller, J. (2022). The intrinsically disordered proteins MLLT3 (AF9) and MLLT1 (ENL)–multimodal transcriptional switches with roles in normal hematopoiesis, MLL fusion leukemia, and kidney cancer. Journal of Molecular Biology, 434(1), 167117.

Liu, C., Li, X., Xiong, F., Wang, L., Chen, K., Wu, P., & Zhang, Z. (2022). Down-regulation of MLLT1 super elongation complex subunit impairs the anti-tumor activity of natural killer cells in esophageal cancer. Immunobiology, 227(4), 152238.

Marei, H. E., Althani, A., Afifi, N., Hasan, A., Caceci, T., Felsani, A., ... & Cenciarelli, C. (2022). Exome sequencing of glioblastoma-derived cancer stem cells reveals rare clinically relevant frameshift deletion in MLLT1 gene. Cancer Cell International, 22(1), 9.

de Matos, R. R., Ferreira, G. M., Meyer, C., Marschalek, R., Larghero, P., Ribeiro, R. C., ... & Silva, M. L. M. (2022). KMT2A-MLLT1 and the Novel SEC16A-KMT2A in a Cryptic 3-Way Translocation t (9; 11; 19) Present in an Infant With Acute Lymphoblastic Leukemia. Journal of Pediatric Hematology/Oncology, 44(3), e719-e722.

Ni, X., Londregan, A. T., Owen, D. R., Knapp, S., & Chaikuad, A. (2021). Structure and inhibitor binding characterization of oncogenic MLLT1 mutants. ACS Chemical Biology, 16(4), 571-578.

Ni, X., Heidenreich, D., Christott, T., Bennett, J., Moustakim, M., Brennan, P. E., ... & Chaikuad, A. (2019). Structural insights into interaction mechanisms of alternative piperazine-urea YEATS domain binders in MLLT1. ACS medicinal chemistry letters, 10(12), 1661-1666.

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

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