Mouse Recombinant HDAC11, Active protein, GST Tag (V2LY-0526-LY8386)

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Basic Information

Expressed Host
Baculovirus-Insect Cells
Protein Species
Mouse
Tag
GST Tag
Protein Construction
This product is Mouse Recombinant HDAC11, Active protein, GST Tag consist of Amino Acid: Full Length and predicts a molecular mass of 66 kDa.
Molecule Mass
66 kDa
Sequence
Amino Acid: Full Length
Species
Mouse

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

Purity
Batch dependent.
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
Tris, NaCl
Preservative
None
Storage
Store product at -70°C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
More Infomation

Target

Full Name
Histone Deacetylase 11
Function
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Biological Process
Chromatin organization Source: UniProtKB
Histone deacetylation Source: UniProtKB
Oligodendrocyte development Source: Ensembl
Cellular Location
Nucleus

Chen, H., Xie, C., Chen, Q., & Zhuang, S. (2022). HDAC11, an emerging therapeutic target for metabolic disorders. Frontiers in Endocrinology, 13, 989305.

Yao, F., Jin, Z., Zheng, Z., Lv, X., Ren, L., Yang, J., ... & Lin, R. (2022). HDAC11 promotes both NLRP3/caspase-1/GSDMD and caspase-3/GSDME pathways causing pyroptosis via ERG in vascular endothelial cells. Cell death discovery, 8(1), 112.

Wen, Y., Zhang, X., Li, X., Tian, L., Shen, S., Ma, J., & Ai, F. (2022). Histone deacetylase (HDAC) 11 inhibits matrix metalloproteinase (MMP) 3 expression to suppress colorectal cancer metastasis. Journal of Cancer, 13(6), 1923.

Bi, L., Ren, Y., Feng, M., Meng, P., Wang, Q., Chen, W., ... & Wang, Y. (2021). HDAC11 regulates glycolysis through the LKB1/AMPK signaling pathway to maintain hepatocellular carcinoma stemness. Cancer Research, 81(8), 2015-2028.

Bora-Singhal, N., Mohankumar, D., Saha, B., Colin, C. M., Lee, J. Y., Martin, M. W., ... & Chellappan, S. (2020). Novel HDAC11 inhibitors suppress lung adenocarcinoma stem cell self-renewal and overcome drug resistance by suppressing Sox2. Scientific reports, 10(1), 4722.

Liu, S. S., Wu, F., Jin, Y. M., Chang, W. Q., & Xu, T. M. (2020). HDAC11: a rising star in epigenetics. Biomedicine & pharmacotherapy, 131, 110607.

Wang, W., Ding, B., Lou, W., & Lin, S. (2020). Promoter hypomethylation and miR-145-5p downregulation-mediated HDAC11 overexpression promotes sorafenib resistance and metastasis of hepatocellular carcinoma cells. Frontiers in cell and developmental biology, 8, 724.

Heim, C. E., Bosch, M. E., Yamada, K. J., Aldrich, A. L., Chaudhari, S. S., Klinkebiel, D., ... & Kielian, T. (2020). Lactate production by Staphylococcus aureus biofilm inhibits HDAC11 to reprogramme the host immune response during persistent infection. Nature microbiology, 5(10), 1271-1284.

Cao, J., Sun, L., Aramsangtienchai, P., Spiegelman, N. A., Zhang, X., Huang, W., ... & Lin, H. (2019). HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2. Proceedings of the National Academy of Sciences, 116(12), 5487-5492.

Yanginlar, C., & Logie, C. (2018). HDAC11 is a regulator of diverse immune functions. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1861(1), 54-59.

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

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