Recombinant Human Histone Deacetylase 1 (HDAC1) Protein (His-SUMO)

Name: Recombinant Human Histone Deacetylase 1 (HDAC1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04299P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HDAC1.

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Product Overview

Description	Recombinant Human Histone Deacetylase 1 (HDAC1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13547
Target Symbol	HDAC1
Synonyms	DKFZp686H12203; GON 10; HD1; HDAC 1; HDAC1; HDAC1_HUMAN; Histone deacetylase 1; Reduced potassium dependency yeast homolog like 1; RPD3; RPD3L1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
Expression Range	1-482aa
Protein Length	Full Length
Mol. Weight	71.1kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.
Subcellular Location	Nucleus.
Protein Families	Histone deacetylase family, HD type 1 subfamily
Database References	HGNC: 4852 OMIM: 601241 KEGG: hsa:3065 STRING: 9606.ENSP00000362649 UniGene: Hs.88556
Tissue Specificity	Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.

Gene Functions References

HDAC1,2 inhibitor either alone or when combined with doxorubicin decreases leukemia burden. PMID: 28579617
miR-34a exhibited suppressive effects on ovarian cancer (OC) cells via directly binding and downregulating HDAC1 expression, which subsequently decreased the resistance to cisplatin and suppressed proliferation in OC cells. PMID: 29561664
Study identified HDAC1, a key regulator of eukaryotic gene expression and many important cellular events, including cell proliferation, differentiation, cancer and immunity, as an interacting partner of ABIN1. PMID: 29058807
r meta-analysis demonstrated an association between increased HDAC1 expression and better OS in Asian breast cancer patients PMID: 29738697
Daxx directly binds to the DNA-binding domain of Slug, impeding histone deacetylase 1 (HDAC1) recruitment and antagonizing Slug E-box binding. This, in turn, stimulates E-cadherin and occludin expression and suppresses Slug-mediated epithelial-mesenchymal transition (EMT) and cell invasiveness. PMID: 28004751
the knockdown of HDAC1/2 upregulated KLF5 protein but not KLF5 mRNA, and the increase in KLF5 protein level by silencing HDAC1/2 was at least in part due to decreased proteasomal degradation. PMID: 29679567
HDAC1 knockdown by siRNA suppressed cell proliferation, and increased apoptosis and chemosensitivity by downregulating c-Myc and upregulating miR-34a. PMID: 30071534
The HDAC1 expression was associated with the SNAIL expression in clinical samples. PMID: 29917299
data show that Hdac1 and Hdac2 impact on Emu-myc B cell proliferation and apoptosis and suggest that a critical level of Hdac activity may be required for Emu-myc tumorigenesis and proper B cell development PMID: 27886239
Data show there is allosteric communication between the inositol-binding site and the active sites in histone deacetylases HDAC1 and HDAC3. PMID: 27109927
High HDAC1 expression is associated with gastrointestinal malignancy. PMID: 28424407
Results show that proteasomal degradation of HDAC1 and HDAC3 by Vpr counteracts HIV-1 latency to reactivate the viral promoter. PMID: 27550312
concomitant LSD1 and HDAC inhibition synergistically induces cell death in rhabdomyosarcoma cells by shifting the ratio of pro- and antiapoptotic BCL-2 proteins in favor of apoptosis, thereby engaging the intrinsic apoptotic pathway PMID: 28617441
Hdac1 levels are increased in blood samples from patients with schizophrenia who had encountered early life stress (ELS), compared with patients without ELS experience. PMID: 28533418
HDAC1 and HDAC2 suppress the expression of PPP2R3A/PR130, a regulatory subunit of the trimeric serine/threonine phosphatase 2 (PP2A). PMID: 29472538
HDAC1 may therefore be considered an unfavorable progression indicator for glioma patients, and may also serve as a potential therapeutic target. PMID: 28624794
new basis of DDX23-Linc00630-HDAC1 signal axis for understanding its pathogenicity, which could be further developed as a valuable therapeutic strategy PMID: 28473661
Results show that histone deacetylase 1 (HDAC1) expression was positively correlated with YY1 transcription factor (YY1) in hepatocellular carcinoma (HCC) cell lines and primary tumor tissues. PMID: 28489564
the combination of p63-positive and HDAC1-negative expressions can be a potential new way for distinguishing epidermal stem cells. PMID: 28672879
Nuclear HDAC2 immunopositivity was significantly higher in actinic cheilitis (AC) when compared with lip squamous cell carcinoma (LSCC). HDAC1 and HAT1 nuclear immunostaining were higher in AC, with no statistical significance. When comparing data with our previous study, we found a positive correlation between HDAC1 X DNMT1/DNMT3b, HDAC2 X DNMT3b, and HAT1 X DNMT1/DNMT3b for certain studied groups. PMID: 28107582
data reveal the mechanism by which chromatin remodeling and target gene expression are regulated by Ikaros alone and in complex with HDAC1 in B-ALL PMID: 26639180
Histone deacetylases 1 and 2 cooperate in regulating BRCA1, CHK1, and RAD51 expression in acute myeloid leukemia cells. PMID: 28030834
our findings identify a key role for c-Myc in TRAIL deregulation and as a biomarker of the anticancer action of HDACi in acute myeloid leukemia . PMID: 27358484
The authors found that 2-aminoacetophenone regulates histone deacetylase 1 expression and activity, resulting in hypo-acetylation of lysine 18 of histone H3 at pro-inflammatory cytokine loci. Specifically, 2-aminoacetophenone induced reprogramming of immune cells occurs via alterations in histone acetylation of immune cytokines in vivo and in vitro. PMID: 27694949
Histone deacetylases (HDACs) inhibitor MGCD0103 (MGCD) induces apoptosis by up-regulating p53 in CNE2 nasopharyngeal carcinoma (NPC) cells. PMID: 27283770
Our findings suggest that up-regulation of UVRAG by HDAC1 inhibition potentiates DNA-damage-mediated cell death in colorectal cancer cells PMID: 29277783
The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 in the development of progression hepatocellular carcinoma. PMID: 27060025
HDAC1 promoted migration and invasion of gallbladder tumor cells by binding with TCF12 to promote epithelial mesenchymal transformation. PMID: 27092878
HDAC1 depletion-induced p53 expression alters cardiac-derived mesenchymal stromal cell fate decisions. PMID: 27501845
These results are the first evidence that the inhibition of HDAC1 by (S)-2 downregulates CIP2A transcription PMID: 27029072
data showed that HDAC1 can trigger the proliferation and migration of breast cancer cells via activation of Snail/IL-8 signals PMID: 28779562
Mechanical stimulation orchestrates the osteogenic differentiation of human bone marrow stromal cells by regulating HDAC1 PMID: 27171263
High HDAC1 expression is associated with Multidrug Resistance in breast and cervical cancer. PMID: 28716899
these results suggest that HDAC1 and HDAC6 may play a role in clear cell renal cell carcinoma biology PMID: 27506904
Histone deacetylase 1 regulates the expression of progesterone receptor A during human parturition by occupying the progesterone receptor A promoter. PMID: 26758364
High HDAC1 expression may contribute to the aggressiveness of human breast cancer with cytoplasmic-only expression of maspin PMID: 28870936
Results indicate that HCV core induced epithelial-mesenchymal transition (EMT) by interacting with the transcriptional repressor complex Snail/HDAC1/2 at the E-cadherin promoter, which led to E-cadherin repression and increased invasiveness of hepatoma cells. PMID: 26549030
Coexpression of SALL4 with HDAC1 and/or HDAC2 was associated with PTEN underexpression and a poor prognosis in hepatocellular carcinoma. PMID: 28411180
Acetylation-dependent control of global poly(A) RNA degradation by CBP/p300 and HDAC1-HDAC2 has been described. PMID: 27635759
Meta-analysis results suggest that HDAC1 mRNA or protein expression may serve as a good diagnostic and prognostic marker for lung cancer. PMID: 28767587
Histone deacetylase assays confirmed that MIER2, but not MIER3 complexes, have associated deacetylase activity. PMID: 28046085
High HDAC1 expression is associated with drug Resistance in Malignant Melanoma. PMID: 26980768
HDAC1 overexpression is associated with Breast Cancer. PMID: 27197203
Data suggest that epigenetic changes in histone acetylation and DNA methylation may contribute to the repression of RGS2 (regulator of G-protein signaling 2) expression in chemo-resistant ovarian cancer cells; regulation of HDAC1 (histone deacetylase 1) and DNMT1 (DNA methyltransferase 1) contribute to the suppression of RGS2. PMID: 28102109
class I HDACs (HDAC1, 2, 3 and 8) play a major role in regulating extracellular matrix and Epithelial-mesenchymal transition, whereas class IIa HDACs (HDAC4 and 5) are less effective. PMID: 27420561
We found that TCF7L1 recruits the C-terminal binding protein (CtBP) and histone deacetylase 1 (HDAC1) to the DKK4 promoter to repress DKK4 gene expression. In the absence of TCF7L1, TCF7L2 and beta-catenin occupancy at the DKK4 promoter is stimulated and DKK4 expression is increased. These findings uncover a critical role for TCF7L1 in repressing DKK4 gene expression to promote the oncogenic potential of CRCs. PMID: 28450117
Using mass spectrometry and site directed mutagenesis, a new Sp1 phosphorylation site Ser702 was defined to be associated with Sp1-HDAC1 interaction and may be important in SR-BI activation, shedding light on the knowledge of delicate mechanism of hepatic HDL receptor SR-BI gene modulation by LDL. PMID: 27320013
findings indicate that WRN interacts with HDACs 1 and 2 to facilitate activity of stalled replication forks under conditions of replication stress. PMID: 27672210
HDAC1- and SRC-mediated phosphorylation of RUNX3 induced by oxidative stress is associated with the cytoplasmic localization of RUNX3 and can lead to RUNX3 inactivation and carcinogenesis. PMID: 27990641
Cutaneous T-cell lymphoma (CTCL) pathogenesis remains unknown, and there are no curative therapies. Our findings not only demonstrate a critical role for IL15-mediated inflammation in cutaneous T-cell lymphomagenesis, but also uncover a new oncogenic regulatory loop in CTCL involving IL15, HDAC1, HDAC6, and miR-21 that shows differential sensitivity to isotype-specific HDAC inhibitors PMID: 27422033

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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.

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