Human HDAC11 ELISA Kit (V2LY-0626-LY2363)

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Tested Data
Request for COA
Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Sensitivity
0.0012 ng/mL
Detection Range
0.02-7 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
39.2 kDa
Components
  • Pre-coated ELISA Plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

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

Storage
Store at 2-8°C
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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