HDAC4+5+9 Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human HDAC4+5+9 Source: E.coli
Amino Acid Sequence: QDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKL Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
HDAC4 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10-100 molar excess
|
Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP3-21347. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
Theoretical MW |
27 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
PBS and 1M Urea, pH 7.4. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for HDAC4+5+9 Recombinant Protein Antigen
Background
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. HDAC9 has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. HDAC5 is a member of the class II mammalian histone deacetylase family, which is structurally related to yeast HDA1. Human HDAC5 is composed of 1122 amino acid residues. The deacetylase domain of HDAC5 is located at the C-terminal half of the molecule. The N-terminal non-deacetylase domain does not show any significant homology with any published sequence.Both domains are required for HDAC5-mediated repression of gene transcription. HDAC5 interacts with a growing number of transcriptional factors including MEF2A as well as other HDAC proteins. The interacting complexes bind to specific regions of chromatin and regulate gene transcription in these regions. HDAC4 is a class II histone deacetylase containing 1084 amino acid residues. HDAC4 has been shown to interact with NCoR. HDAC4 is a member of the class II mammalian histone deacetylases, which consists of 1084 amino acid residues. Its C terminal sequence is highly similar to the deacetylase domain of yeast HDA1. HDAC4, unlike other deacetylases, shuttles between the nucleus and cytoplasm in a process involving active nuclear export. Association of HDAC4 with 14-3-3 results in sequestration of HDAC 4 protein in the cytoplasm. In the nucleus, HDAC4 associates with the myocyte enhancer factor MEF2A. Binding of HDAC4 to MEF2A results in the repression of MEF2A transcriptional activation. HDAC4 has also been shown to interact with other deacetylases such as HDAC3 as well as the corepressors NcoR and SMART.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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