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Mouse Anti-MLLT3 (AA 1-568) Recombinant Antibody (CBFYM-2307) (CBMAB-M2492-FY)

This product is mouse antibody that recognizes MLLT3. The antibody CBFYM-2307 can be used for immunoassay techniques such as: ELISA, WB.
See all MLLT3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2307
Antibody Isotype
IgG2a, k
Application
ELISA, WB

Basic Information

Immunogen
Full length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: MASSCAVQVK LELGHRAQVR KKPTVEGFTH DWMVFVRGPE HSNIQHFVEK VVFHLHESFP RPKRVCKDPP YKVEESGYAG FILPIEVYFK NKEEPRKVRF DYDLFLHLEG HPPVNHLRCE KLTFNNPTED FRRKLLKAGG D
Specificity
Human
Antibody Isotype
IgG2a, k
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 1-568

Target

Full Name
MLLT3
Introduction
MLLT3 is a Protein Coding gene. Diseases associated with MLLT3 include Acute Myeloid Leukemia With T and Leukemia. 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 MLLT1.
Entrez Gene ID
4300
UniProt ID
P42568
Alternative Names
MLLT3, Super Elongation Complex Subunit; Myeloid/Lymphoid Or Mixed-Lineage Leukemia Translocated To Chromosome 3 Protein; ALL1-Fused Gene From Chromosome 9 Protein; YEATS Domain-Containing Protein 3; YEATS3; AF9
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, PubMed:25417107, PubMed:27105114, PubMed:27545619).

Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated (PubMed:25417107, PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749).

Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25417107, PubMed:27105114, PubMed:27545619).

Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).

Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3 (PubMed:25417107, PubMed:27105114, PubMed:30385749).

In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones (PubMed:27105114, PubMed:27545619).

Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me) (PubMed:25417107).

Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than confering, HSC stemness (PubMed:31776511).

Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L (PubMed:31776511).
Biological Process
Anterior/posterior pattern specification Source: Ensembl
Chromatin remodeling Source: GO_Central
Gene expression Source: Ensembl
Hematopoietic stem cell differentiation Source: UniProtKB
Histone acetylation Source: GO_Central
Negative regulation of canonical Wnt signaling pathway Source: MGI
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI
Regulation of chromatin organization Source: UniProtKB
Regulation of stem cell division Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central
Segment specification Source: Ensembl
Cellular Location
Nucleus
Other locations
Chromosome
Note: Colocalizes with acylated histone H3 (PubMed:25417107, PubMed:27105114). Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).
Involvement in disease
A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204).
A chromosomal aberration involving MLLT3 was observed in a patient with neuromotor development delay, cerebellar ataxia and epilepsy. Translocation t(4;9)(q35;p22).

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.

Gao, L., Lu, J., Li, J., Hu, Y., Lu, Y., Du, W., & Hu, S. (2023). Lineage switch in a pediatric patient with KMT2A-MLLT3 from acute megakaryoblastic leukemia to T cell acute lymphoblastic leukemia at the fourth relapse after allo-HSCT: with literature review. International Journal of Hematology, 117(5), 781-785.

Germano, G., Porazzi, P., & Felix, C. A. (2022). Leukemia‐associated transcription factor mllt3 is important for primitive erythroid development in zebrafish embryogenesis. Developmental Dynamics, 251(10), 1728-1740.

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.

Sepúlveda-Robles, O., Jiménez-Hernández, E., Domínguez-Catzín, V., Gómez-Flores, E., Martín-Trejo, J. A., Flores-Lujano, J., ... & Mejía-Aranguré, J. M. (2022). Analytical study of RUNX1-RUNXT1, PML-RARA, CBFB-MYH11, BCR-ABL1p210, and KMT2-MLLT3 in Mexican children with acute myeloid leukemia: A multicenter study of the Mexican interinstitutional group for the identification of the causes of childhood leukemia (MIGICCL). Frontiers in Pediatrics, 10, 946690.

Gagnon, M. F., Smadbeck, J. B., Sharma, N., Blackburn, P. R., Demasi Benevides, J., Akkari, Y. M., ... & Baughn, L. B. (2022). Apparent coexistence of ETV6:: RUNX1 and KMT2A:: MLLT3 fusions due to a nonproductive KMT2A rearrangement in B-ALL. Leukemia & Lymphoma, 63(9), 2243-2246.

Cui, Y., Zhou, M., Zou, P., Liao, X., & Xiao, J. (2021). Mature B cell acute lymphoblastic leukaemia with KMT2A-MLLT3 transcripts in children: three case reports and literature reviews. Orphanet Journal of Rare Diseases, 16, 1-10.

Panagopoulos, I., Andersen, K., Eilert-Olsen, M., Zeller, B., Munthe-Kaas, M. C., Buechner, J., ... & Heim, S. (2021). Therapy-induced deletion in 11q23 leading to fusion of KMT2A with ARHGEF12 and development of B lineage acute lymphoplastic leukemia in a child treated for acute myeloid leukemia caused by t (9; 11)(p21; q23)/KMT2A-MLLT3. Cancer Genomics & Proteomics, 18(1), 67-81.

Wang, C. I., Kao, H. K., Chen, T. W., Huang, Y., Cheng, H. W., Yi, J. S., ... & Chang, K. P. (2019). Characterization of copy number variations in Oral cavity squamous cell carcinoma reveals a novel role for MLLT3 in cell invasiveness. The Oncologist, 24(12), e1388-e1400.

Calvanese, V., Nguyen, A. T., Bolan, T. J., Vavilina, A., Su, T., Lee, L. K., ... & Mikkola, H. K. (2019). MLLT3 governs human haematopoietic stem-cell self-renewal and engraftment. Nature, 576(7786), 281-286.

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

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