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Rabbit Anti-ASXL2 Recombinant Antibody (CBYC-A830) (CBMAB-A3827-YC)


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Summary

Host Animal
Rabbit
Specificity
Human, Monkey
Clone
CBYC-A830
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Synthetic peptide corresponding to residues surrounding Ala640 of human ASXL2 protein.
Host Species
Mouse
Specificity
Human, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000

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

Format
Liquid
Buffer
HEPES, pH 7.5, 100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Additional Sex Combs Like 2, Transcriptional Regulator
Introduction
ASXL2 is a member of a family of epigenetic regulators that bind various histone-modifying enzymes and are involved in the assembly of transcription factors at specific genomic loci. Naturally occurring mutations in this gene are associated with cancer in
Entrez Gene ID
55252
UniProt ID
Q76L83
Alternative Names
Additional Sex Combs Like 2, Transcriptional Regulator; Additional Sex Combs-Like Protein 2; ASXH2; Additional Sex Combs Like 2 (Drosophila); Putative Polycomb Group Protein ASXL2; Polycomb Group Protein ASXH2; KIAA1685; SHAPNS;
Function
Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity).
Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3.
Biological Process
Animal organ morphogenesis Source: GO_Central
Positive regulation of fat cell differentiation Source: UniProtKB
Positive regulation of lipid storage Source: Ensembl
Positive regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Protein deubiquitination Source: Reactome
Transcription, DNA-templated Source: InterPro
Cellular Location
Nucleus
Involvement in disease
Shashi-Pena syndrome (SHAPNS): An autosomal dominant syndrome characterized by delayed psychomotor development, intellectual disability of variable severity, macrocephaly, prominent eyes, arched eyebrows, hypertelorism, a glabellar nevus flammeus, neonatal feeding difficulties, and hypotonia. Some patients may also have atrial septal defect, episodic hypoglycemia, changes in bone mineral density, and/or seizures.
More Infomation

Peng, H., Cassel, J., McCracken, D. S., Prokop, J. W., Sementino, E., Cheung, M., ... & Rauscher, F. J. (2021). Kinetic Characterization of ASXL1/2-Mediated Allosteric Regulation of the BAP1 Deubiquitinase. Molecular Cancer Research.

Zhang, P., Xu, M., & Yang, F. C. (2020). The role of ASXL1/2 and their associated proteins in malignant hematopoiesis. Current Stem Cell Reports, 6(1), 6-15.

Kolovos, P., Nishimura, K., Sankar, A., Sidoli, S., Cloos, P. A., Helin, K., & Christensen, J. (2020). PR-DUB maintains the expression of critical genes through FOXK1/2-and ASXL1/2/3-dependent recruitment to chromatin and H2AK119ub1 deubiquitination. Genome research, 30(8), 1119-1130.

Cui, R., Yang, L., Wang, Y., Zhong, M., Yu, M., & Chen, B. (2020). Elevated Expression of ASXL2 is Associated with Poor Prognosis in Colorectal Cancer by Enhancing Tumorigenesis and Inducing Cell Proliferation. Cancer Management and Research, 12, 10221.

Peng, H., Prokop, J., Karar, J., Park, K., Cao, L., Harbour, J. W., ... & Rauscher, F. J. (2018). Familial and somatic BAP1 mutations inactivate ASXL1/2-mediated allosteric regulation of BAP1 deubiquitinase by targeting multiple independent domains. Cancer research, 78(5), 1200-1213.

Madan, V., Han, L., Hattori, N., Teoh, W. W., Mayakonda, A., Sun, Q. Y., ... & Koeffler, H. P. (2018). ASXL2 regulates hematopoiesis in mice and its deficiency promotes myeloid expansion. haematologica, 103(12), 1980.

Micol, J. B., Pastore, A., Inoue, D., Duployez, N., Kim, E., Lee, S. C. W., ... & Abdel-Wahab, O. (2017). ASXL2 is essential for haematopoiesis and acts as a haploinsufficient tumour suppressor in leukemia. Nature communications, 8(1), 1-13.

Jahn, N., Agrawal, M., Bullinger, L., Weber, D., Corbacioglu, A., Gaidzik, V. I., ... & Paschka, P. (2017). Incidence and prognostic impact of ASXL2 mutations in adult acute myeloid leukemia patients with t (8; 21)(q22; q22): a study of the German-Austrian AML Study Group. Leukemia, 31(4), 1012-1015.

Oak, J. S., & Ohgami, R. S. (2017). Focusing on frequent ASXL1 mutations in myeloid neoplasms, and considering rarer ASXL2 and ASXL3 mutations.

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

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