Mouse Recombinant HDAC8 protein, His Tag (V2LY-0526-LY8389)

Name: Mouse Recombinant HDAC8 protein, His Tag
SKU: V2LY-0526-LY8389
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

Baculovirus-Insect Cells

Protein Species

Mouse

Tag

His Tag

Protein Construction

This product is Mouse Recombinant HDAC8 protein, His Tag consist of Amino Acid: 1-377 and predicts a molecular mass of 43.1 kDa.

Molecule Mass

43.1 kDa

Sequence

Amino Acid: 1-377

Species

Mouse

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

Purity

>90% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile Tris, NaCl

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

HDAC8

Function

Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, PubMed:28497810).

Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748).

Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748).

Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700).

May play a role in smooth muscle cell contractility (PubMed:15772115).

In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810).

Biological Process

Chromatin assembly or disassembly Source: ProtInc
Chromatin organization Source: UniProtKB
Histone H3 deacetylation Source: GO_Central
Histone H4 deacetylation Source: GO_Central
Negative regulation of protein ubiquitination Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: ProtInc
Positive regulation of transcription by RNA polymerase II Source: GO_Central
Regulation of cohesin loading Source: UniProtKB
Regulation of protein stability Source: BHF-UCL
Regulation of telomere maintenance Source: BHF-UCL
Sister chromatid cohesion Source: UniProtKB

Cellular Location

Nucleus; Cytoplasm; Chromosome. Excluded from the nucleoli (PubMed:10748112). Found in the cytoplasm of cells showing smooth muscle differentiation (PubMed:15772115, PubMed:16538051).

Involvement in disease

Cornelia de Lange syndrome 5 (CDLS5):
A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.

PTM

Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4.

Kim, J. Y., Cho, H., Yoo, J., Kim, G. W., Jeon, Y. H., Lee, S. W., & Kwon, S. H. (2022). Pathological role of HDAC8: Cancer and beyond. Cells, 11(19), 3161.

Fontana, A., Cursaro, I., Carullo, G., Gemma, S., Butini, S., & Campiani, G. (2022). A therapeutic perspective of HDAC8 in different diseases: an overview of selective inhibitors. International Journal of Molecular Sciences, 23(17), 10014.

Yang, W., Feng, Y., Zhou, J., Cheung, O. K. W., Cao, J., Wang, J., ... & Cheng, A. S. L. (2021). A selective HDAC8 inhibitor potentiates antitumor immunity and efficacy of immune checkpoint blockade in hepatocellular carcinoma. Science translational medicine, 13(588), eaaz6804.

Sawada, Y., Nakatsuji, T., Dokoshi, T., Kulkarni, N. N., Liggins, M. C., Sen, G., & Gallo, R. L. (2021). Cutaneous innate immune tolerance is mediated by epigenetic control of MAP2K3 by HDAC8/9. Science immunology, 6(59), eabe1935.

Spreafico, M., Gruszka, A. M., Valli, D., Mazzola, M., Deflorian, G., Quintè, A., ... & Pistocchi, A. (2020). HDAC8: a promising therapeutic target for acute myeloid leukemia. Frontiers in Cell and Developmental Biology, 8, 844.

Hassan, M. M., Israelian, J., Nawar, N., Ganda, G., Manaswiyoungkul, P., Raouf, Y. S., ... & Gunning, P. T. (2020). Characterization of conformationally constrained benzanilide scaffolds for potent and selective HDAC8 targeting. Journal of Medicinal Chemistry, 63(15), 8634-8648.

An, P., Chen, F., Li, Z., Ling, Y., Peng, Y., Zhang, H., ... & Wang, H. (2020). HDAC8 promotes the dissemination of breast cancer cells via AKT/GSK-3β/Snail signals. Oncogene, 39(26), 4956-4969.

Saito, S., Zhuang, Y., Suzuki, T., Ota, Y., Bateman, M. E., Alkhatib, A. L., ... & Lasky, J. A. (2019). HDAC8 inhibition ameliorates pulmonary fibrosis. American Journal of Physiology-Lung Cellular and Molecular Physiology, 316(1), L175-L186.

Zhao, C., Zang, J., Inks, E. S., Xu, W., Chou, C. J., & Zhang, Y. (2018). Discovery of meta-sulfamoyl N-hydroxybenzamides as HDAC8 selective inhibitors. European Journal of Medicinal Chemistry, 150, 282-291.

Amin, S. A., Adhikari, N., & Jha, T. (2018). Structure-activity relationships of HDAC8 inhibitors: non-hydroxamates as anticancer agents. Pharmacological Research, 131, 128-142.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Alternative Versions

Human Recombinant HDAC8, Active protein, GST Tag (CAT#: V2LY-0526-LY4473)

Human Recombinant HDAC8, Active protein, His Tag (CAT#: V2LY-0526-LY4474)

Human Recombinant HDAC8 protein, GST Tag (CAT#: V2LY-0526-LY4475)

Human HDAC8 ELISA Kit (CAT#: V2LY-0626-LY1309)

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Human Recombinant HDAC8, Active protein, His Tag (CAT#: V2LY-0526-LY4474)

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Human HDAC8 ELISA Kit (CAT#: V2LY-0626-LY1309)

Mouse Anti-HDAC8 Recombinant Antibody (CBFYH-0894) (CAT#: CBMAB-H1823-FY)

Isotype control

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

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