Recombinant Human HDAC11 Protein

Name: Recombinant Human HDAC11 Protein
Brand: Beta LifeScience
SKU: BL-0238SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_024827
Synonym	FLJ22237; HD11
Background	HDAC11 belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. HDAC11 belongs to class IV of the histone deacetylase family that localizes to the nucleus and is involved in regulating the expression of interleukin 10 (1). HDAC11 expression is the highest in brain, heart, skeletal muscle, kidney and testis. HDAC11 control the DNA expression by modifying the core histone octamers that package DNA into dense chromatin structures and repress gene expression. HDAC11 has HDAC activity and this activity is inhibitable by trapoxin, an HDAC inhibitor (2). In coimmunoprecipitation experiments, HDAC11 interacts with HDA6.
Description	Recombinant full length human HDAC11 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~66 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human HDAC11 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
Subcellular Location	Nucleus. Note=Predominantly nuclear.
Protein Families	Histone deacetylase family
Database References	HGNC: 19086 OMIM: 607226 KEGG: hsa:79885 STRING: 9606.ENSP00000295757 UniGene: Hs.744132
Tissue Specificity	Weakly expressed in most tissues. Strongly expressed in brain, heart, skeletal muscle, kidney and testis.

Gene Functions References

The results indicated that HDAC11 was significantly expressed in human and mouse diabetic heart failure (DHF) hearts. PMID: 29655790
Mycobacterium tuberculosis infection disturbs the HDAC6/HDAC11 levels to induce IL-10 expression in macrophages. PMID: 29523311
HDAC11 was initially identified as a negative regulator of the well-known anti-inflammatory cytokine IL-10. Hence, antagonizing HDAC11 activity may have anti-tumor potential, whereas activating HDAC11 may be useful to treat chronic inflammation or autoimmunity. PMID: 29222071
Results showed that the high levels of HDAC11 and lower levels of p53 were detected in pituitary tumor cells. A negative correlation was detected between the data of HDAC11 and p53. PMID: 28782861
Our study identified a group of cell cycle-promoting genes regulated by HDAC11. PMID: 28252645
High HDAC11 expression is associated with neoplasms. PMID: 23024001
Data indicate a pronounced deregulation of HDAC genes HDAC9 and HDAC11 in patients with Philadelphia-negative chronic myeloproliferative neoplasms: essential thrombocythemia (ET), polycythemia vera (PV) and primary myelofibrosis (PMF). PMID: 21806350
These results demonstrate for the first time that HDAC11 plays an essential role in regulating OX40L expression. PMID: 21239696
HDAC11 associates with replication origins inhibits Cdt1-induced re-replication and suppresses MCM loading. PMID: 20980834
We found a reduction of HDAC 11 mRNA and increased HDAC 2 levels in amyotrophic lateral sclerosis brain and spinal cord compared with controls. PMID: 20467334
cloning and functional characterization PMID: 11948178
Fluorescence in situ hybridization analysis localized HDAC11 gene to chromosome 3p25, a region characterized by frequent gains and losses of chromosomal material in a number of various types of cancer. PMID: 16142391
the absence of tumour-specific somatic events in WNT7A and HDAC11 suggests that these genes are unlikely to have a classical tumour suppressor gene role in sporadic malignant pancreatic endocrine tumours PMID: 17201809
HDAC11 negatively regulated expression of the gene encoding interleukin 10 in antigen-presenting cells. PMID: 19011628
Cdt1 undergoes acetylation and is reversibly deacetylated by HDAC11 PMID: 19276081

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.