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AB42632

Recombinant human HDAC6 protein (Active) (GST tag N-Terminus)

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(4 Publications)

Recombinant human HDAC6 protein (Active) (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 1215 aa range, expressed in Baculovirus infected Sf9 cells, with >65%, suitable for SDS-PAGE, FuncS, Inhib.

View Alternative Names

KIAA0901, JM21, HDAC6, Protein deacetylase HDAC6, E3 ubiquitin-protein ligase HDAC6, Tubulin-lysine deacetylase HDAC6

2 Images
Functional Studies - Recombinant human HDAC6 protein (Active) (GST tag N-Terminus) (AB42632)
  • FuncS

Supplier Data

Functional Studies - Recombinant human HDAC6 protein (Active) (GST tag N-Terminus) (AB42632)

Specific Activity : ≥350 pmol/min/μg.

Assay Conditions : 25 mM Tris/HCl, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2, and 0.1 mg/ml BSA, 20 μM BPS HDAC substrate 3, and HDAC6 (3.1 – 200 ng). Incubation condition : 30 min at 37°C followed by developing for 15 min at room temperature.

SDS-PAGE - Recombinant human HDAC6 protein (Active) (GST tag N-Terminus) (AB42632)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human HDAC6 protein (Active) (GST tag N-Terminus) (AB42632)

4-20% SDS-PAGE - Recombinant human HDAC6 protein (Active) (ab42632).

Lane 1 : 2μg HDAC6.

Lane 2 : MW marker.

Key facts

Purity

>65% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

SDS-PAGE, Inhib, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: ≥350 pmol/min/μg.

Assay Conditions: 25 mM Tris/HCl, pH 8.0, 137 mM NaCl, 2.7 mM KCl, 1 mM MgCl2, and 0.1 mg/ml BSA, 20 μM BPS HDAC substrate 3, and HDAC6 (3.1 – 200 ng). Incubation condition: 30 min at 37°C followed by developing for 15 min at room temperature.

Accession

Q9UBN7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.04% Sorbitan monolaurate, ethoxylated, 0.0165% Potassium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Inhib": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Use at an assay dependent dilution. Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.</p>" } } }

Sequence info

[{"sequence":"MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDPMGHHHHHHGRRRASVAAGILVPRGSPGLDGIYARGIQMTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH","proteinLength":"Full Length","predictedMolecularWeight":"161 kDa","actualMolecularWeight":null,"aminoAcidEnd":1215,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"Q9UBN7","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

HDAC6 or histone deacetylase 6 is a protein that primarily functions as a cytoplasmic deacetylase. It is part of the class IIb HDAC family and is known for its distinctive molecular weight of approximately 121 kDa. HDAC6 is expressed in various tissues with higher levels observed in the brain kidney and liver. This protein is unique as it contains two catalytic domains unlike other HDACs which contributes to its specific deacetylation of non-histone substrates including tubulin and Hsp90 influencing cell motility and stress response.
Biological function summary

HDAC6 plays a significant role in processes like protein degradation and cell signaling. It is an important component of the protein quality control system involving itself in the aggresome pathway where it facilitates the removal of misfolded proteins through interaction with dynein motor proteins. In addition to its presence in the cytoplasm HDAC6 influences cell migration and immune response regulation by de-phosphorylating cortactin and affecting actin filament dynamics. Its integral role in the aggresome-autophagy pathway positions it as important for cellular homeostasis maintenance.

Pathways

HDAC6 participates prominently in both autophagy and stress response pathways. In the autophagic process HDAC6 operates alongside ubiquitinated proteins to manage protein quality control. Moreover HDAC6 engages in stress response pathways like the heat shock response interacting directly with Hsp90 to regulate client protein activation. These pathways highlight HDAC6’s relationships with key proteins such as Hsp70 and tau linking it to cellular stress and neurodegeneration responses.

HDAC6 exhibits connections to neurodegenerative diseases and cancer. Dysregulated HDAC6 activity associates with Alzheimer's disease where it affects tau protein accumulation and degradation. The protein is also implicated in various cancers such as breast and ovarian cancer due to its influence on cell migration and invasion. It interacts with p53 impacting apoptosis and tumor progression making HDAC6 a potential target for therapeutic interventions with HDAC6 inhibitors which aim to restore normal cellular functions disrupted by abnormal HDAC6 activity.

Specifications

Form

Liquid

Additional notes

Protein was purified by affinity chromatography and gel filtration.

General info

Function

Deacetylates a wide range of non-histone substrates (PubMed : 12024216, PubMed : 18606987, PubMed : 20308065, PubMed : 24882211, PubMed : 26246421, PubMed : 30538141, PubMed : 31857589, PubMed : 30770470, PubMed : 38534334, PubMed : 39567688). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed : 12024216, PubMed : 20308065, PubMed : 26246421). Required for cilia disassembly via deacetylation of alpha-tubulin (PubMed : 17604723, PubMed : 26246421). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed : 30538141). Deacetylates SQSTM1 (PubMed : 31857589). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (PubMed : 18606987). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities (PubMed : 24882211). Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage (PubMed : 30770470). Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity). Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis (PubMed : 38534334). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed : 26080397). Deacetylates PRDM16 (By similarity). Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region (PubMed : 39567688). In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage (PubMed : 39567688). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (By similarity). In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins : when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome (PubMed : 17846173). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy (PubMed : 17846173). Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer (PubMed : 24413532).. (Microbial infection) Deacetylates the SARS-CoV-2 N protein which promotes association of the viral N protein with human G3BP1, leading to disruption of cellular stress granule formation and facilitating viral replication.

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Post-translational modifications

Phosphorylated by AURKA; phosphorylation increases HDAC6-mediated deacetylation of alpha-tubulin and subsequent disassembly of cilia.. Ubiquitinated. Its polyubiquitination however does not lead to its degradation.. Sumoylated in vitro.

Subcellular localisation

Cytoskeleton

Product protocols

Target data

Deacetylates a wide range of non-histone substrates (PubMed : 12024216, PubMed : 18606987, PubMed : 20308065, PubMed : 24882211, PubMed : 26246421, PubMed : 30538141, PubMed : 31857589, PubMed : 30770470, PubMed : 38534334, PubMed : 39567688). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed : 12024216, PubMed : 20308065, PubMed : 26246421). Required for cilia disassembly via deacetylation of alpha-tubulin (PubMed : 17604723, PubMed : 26246421). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed : 30538141). Deacetylates SQSTM1 (PubMed : 31857589). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (PubMed : 18606987). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities (PubMed : 24882211). Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage (PubMed : 30770470). Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity). Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis (PubMed : 38534334). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed : 26080397). Deacetylates PRDM16 (By similarity). Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region (PubMed : 39567688). In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage (PubMed : 39567688). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (By similarity). In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins : when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome (PubMed : 17846173). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy (PubMed : 17846173). Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer (PubMed : 24413532).. (Microbial infection) Deacetylates the SARS-CoV-2 N protein which promotes association of the viral N protein with human G3BP1, leading to disruption of cellular stress granule formation and facilitating viral replication.
See full target information HDAC6

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Journal of enzyme inhibition and medicinal chemistry 38:2201408 PubMed37096557

2023

Discovery of novel benzohydroxamate-based histone deacetylase 6 (HDAC6) inhibitors with the ability to potentiate anti-PD-L1 immunotherapy in melanoma.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaopeng Peng,Ziwen Yu,Goverdhan Surineni,Bulian Deng,Meizhu Zhang,Chuan Li,Zhiqiang Sun,Wanyi Pan,Yao Liu,Shenglan Liu,Bin Yu,Jianjun Chen

Journal of medicinal chemistry 61:6056-6074 PubMed29940115

2018

Discovery of Janus Kinase 2 (JAK2) and Histone Deacetylase (HDAC) Dual Inhibitors as a Novel Strategy for the Combinational Treatment of Leukemia and Invasive Fungal Infections.

Applications

Unspecified application

Species

Unspecified reactive species

Yahui Huang,Guoqiang Dong,Huanqiu Li,Na Liu,Wannian Zhang,Chunquan Sheng

European journal of medicinal chemistry 141:596-602 PubMed29102179

2017

Discovery of a fluorescent probe with HDAC6 selective inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

Yingjie Zhang,Jin Yan,Tso-Pang Yao

Journal of medicinal chemistry 58:4325-38 PubMed25906087

2015

Design, synthesis, and antitumor evaluation of novel histone deacetylase inhibitors equipped with a phenylsulfonylfuroxan module as a nitric oxide donor.

Applications

Unspecified application

Species

Unspecified reactive species

Wenwen Duan,Jin Li,Elizabeth S Inks,C James Chou,Yuping Jia,Xiaojing Chu,Xiaoyang Li,Wenfang Xu,Yingjie Zhang
View all publications

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