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Mouse Anti-HOXA9 Recombinant Antibody (CBT3635) (V2LY-0625-LY388)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBT3635
Antibody Isotype
IgG1
Application
ICC, FC

Basic Information

Immunogen
Purified recombinant fragment of human HOXA9 (AA: 1-272) expressed in E. Coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:500-1:2,000
ICC1:200-1:1,000
FC1:200-1:400
ELISA1:10,000

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

Format
Liquid
Buffer
PBS
Preservative
Sodium azide
Concentration
Batch dependent
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
homeobox A9
Entrez Gene ID
3205
UniProt ID
P31269
Function
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation.
Biological Process
Anterior/posterior pattern specification Source: GO_Central
Embryonic skeletal system morphogenesis Source: GO_Central
Endothelial cell activation Source: UniProtKB
Multicellular organism development Source: ProtInc
Negative regulation of myeloid cell differentiation Source: UniProtKB
Proximal/distal pattern formation Source: GO_Central
Regulation of transcription by RNA polymerase II Source: GO_Central
Transcription, DNA-templated Source: InterPro
Cellular Location
Nucleus
Involvement in disease
A chromosomal aberration involving HOXA9 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with NUP98 (PubMed:8563753). The chimera includes NUP98 intrinsic disordered regions which contribute to aberrant liquid-liquid phase separation puncta of the chimera in the nucleus. This phase-separation enhances the chimera genomic targeting and induces organization of aberrant three-dimensional chromatin structures leading to tumourous transformation (PubMed:34163069).
A chromosomal aberration involving HOXA9 may contribute to disease progression in chronic myeloid leukemia. Translocation t(7;17)(p15;q23) with MSI2.
PTM
Methylated on Arg-140 by PRMT5; methylation is critical for E-selectin induction.
More Infomation

Aryal, S., Zhang, Y., Wren, S., Li, C., & Lu, R. (2023). Molecular regulators of HOXA9 in acute myeloid leukemia. The FEBS Journal, 290(2), 321-339.

Talarmain, L., Clarke, M. A., Shorthouse, D., Cabrera-Cosme, L., Kent, D. G., Fisher, J., & Hall, B. A. (2022). HOXA9 has the hallmarks of a biological switch with implications in blood cancers. Nature Communications, 13(1), 5829.

Akirtava, C., May, G. E., & McManus, C. J. (2022). False-positive IRESes from Hoxa9 and other genes resulting from errors in mammalian 5′ UTR annotations. Proceedings of the National Academy of Sciences, 119(36), e2122170119.

Yoshino, S., Yokoyama, T., Sunami, Y., Takahara, T., Nakamura, A., Yamazaki, Y., ... & Nakamura, T. (2021). Trib1 promotes acute myeloid leukemia progression by modulating the transcriptional programs of Hoxa9. Blood, The Journal of the American Society of Hematology, 137(1), 75-88.

Depauw, S., Lambert, M., Jambon, S., Paul, A., Peixoto, P., Nhili, R., ... & David-Cordonnier, M. H. (2019). Heterocyclic diamidine DNA ligands as HOXA9 transcription factor inhibitors: Design, molecular evaluation, and cellular consequences in a HOXA9-dependant leukemia cell model. Journal of medicinal chemistry, 62(3), 1306-1329.

Lynch, J. R., Salik, B., Connerty, P., Vick, B., Leung, H., Pijning, A., ... & Wang, J. Y. (2019). JMJD1C-mediated metabolic dysregulation contributes to HOXA9-dependent leukemogenesis. Leukemia, 33(6), 1400-1410.

Lambert, M., Alioui, M., Jambon, S., Depauw, S., Seuningen, I. V., & David-Cordonnier, M. H. (2019). Direct and indirect targeting of HOXA9 transcription factor in acute myeloid leukemia. Cancers, 11(6), 837.

de Bock, C. E., Demeyer, S., Degryse, S., Verbeke, D., Sweron, B., Gielen, O., ... & Cools, J. (2018). HOXA9 cooperates with activated JAK/STAT signaling to drive leukemia development. Cancer discovery, 8(5), 616-631.

Sun, Y., Zhou, B., Mao, F., Xu, J., Miao, H., Zou, Z., ... & Hess, J. L. (2018). HOXA9 reprograms the enhancer landscape to promote leukemogenesis. Cancer cell, 34(4), 643-658.

Zhou, L., Wang, Y., Zhou, M., Zhang, Y., Wang, P., Li, X., ... & Ding, Z. (2018). HOXA9 inhibits HIF-1α-mediated glycolysis through interacting with CRIP2 to repress cutaneous squamous cell carcinoma development. Nature communications, 9(1), 1480.

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

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