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RABBIT ANTI HISTONE DEACETYLASE 1

ArtNr 18-783-313773
Hersteller GENWAY
Menge 0.05 mg
Kategorie
Typ Antibody
Applikationen WB, IF
Specific against other
Host Rabbit
ECLASS 10.1 32160702
ECLASS 11.0 32160702
UNSPSC 12352203
Alias GWB-7DE68A
Similar products 18-783-313773
Lieferbar
Genway ID:
GWB-7DE68A
Specificity:
HISTONE DEACETYLASE 1
Isotype:
Polyclonal IgGSpecies Cross Reactivity: Reacts with: Bovine ChickenN. B. Antibody reactivity and working conditions may vary between species.
Buffer Solution:
Phosphate buffered saline pH7. 2
Preservative Stabilisers:
0. 01% Sodium Azide (NaN3)Approx. Protein Concentrations: IgG concentration 1. 0mg/ml
Immunogen:
Synthetic peptide corresponding to amino acid sequence 666-482 of Human HDAC-1.
Specificity:
Recognises human histone deacetylase 1 (HDAC1). Histone acetylation and deacetylation play important roles in modifying chromatin structure and regulating eukaryotic gene expression. HDAC1 is a 62kD class I HDAC enzyme which is related to the yeast transcriptional regulator Rpd3p. Recommended Secondary Antibodies: Sheep Anti Rabbit IgGGoat Anti Rabbit IgG (Fc)Goat Anti Rabbit IgG (H/L)
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. Ref. 19Ref. 32Ref. 41Catalytic activityHydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. Subunit structurePart of the core histone deacetylase (HDAC) complex composed of HDAC1 HDAC2 RBBP4 and RBBP7. The core complex associates with MTA2 MBD2 MBD3 MTA1L1 CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex or with SIN3 SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1 HDAC2 HMG20B/BRAF35 KDM1A RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2 ZNF217 ZMYM3 GSE1 and GTF2I. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with BAZ2A/TIP5 BCOR BRMS1L DAXX DNMT1 EP300 HCFC1 NFE4 PCAF PHB2 MIER1 KDM4A MINT NRIP1 PRDM6 RERE SETDB1 SUV39H1 TGIF TGIF2 UHRF1 UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Interacts with HDAC9. Component of a mSin3A corepressor complex that contains SIN3A SAP130 SUDS3/SAP45 ARID4B/SAP180 HDAC1 and HDAC2. Interacts with BANP CBFA2T3 and KDM5B. Interacts with SAP30L. Interacts with E4F1. Interacts with KFL1 By similarity. Interacts with SV40 large T antigen. Interacts with CHFR PRDM16 SP1 SP3 and SMAD3. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6. Ref. 19Ref. 32Ref. 41Ref. 4Ref. 5Ref. 6Ref. 7Ref. 8Ref. 9Ref. 11Ref. 12Ref. 13Ref. 14Ref. 17Ref. 20Ref. 22Ref. 23Ref. 24Ref. 26Ref. 28Ref. 29Ref. 33Ref. 35Ref. 36Ref. 39Ref. 46Ref. 48Subcellular locationNucleus. Tissue specificityUbiquitous with higher levels in heart pancreas and testis and lower levels in kidney and brain. Post-translational modificationSumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. Ref. 15Ref. 16Ref. 25Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Ubiquitinated by CHFR leading to its degradation by the proteasome By similarity. Ref. 48Sequence similaritiesBelongs to the histone deacetylase family. Type 1 subfamily.

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Alle Produkte sind nur für Forschungszwecke bestimmt. Nicht für den menschlichen, tierärztlichen oder therapeutischen Gebrauch.

Menge: 0.05 mg
Lieferbar: In stock
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Lieferung vsl. bis 30.08.2024 

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