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Recombinant Human Bromodomain adjacent to zinc finger domain protein 2A (BAZ2A), partial

Recombinant Human Bromodomain adjacent to zinc finger domain protein 2A (BAZ2A), partial

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

BAZ2A

Purity

>85% (SDS-PAGE)

Target Names

BAZ2A

Uniprot NO.

Q9UIF9

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-1905

Target Protein Sequence

MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPSVAYD CLWNYSQYPS ANPGSNLKDP PLLSQFSGGQ YPLNGILGGS RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL EEEQPELKMC GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA FSLLADDSQT STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ SSDFPPSLTQ PAPDQSSTIQ LHPATSPAVS PTTSPAVSLV VSPAASPEIS PEVCPAASTV VSPAVFSVVS PASSAVLPAV SLEVPLTASV TSPKASPVTS PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD VMRRRIATPE EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG KRGRPRNTEK AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE TLNEEDKAKI AKSKKKMRQK VQRGECQTTI QGQARNKRKQ ETKSLKQKEA KKKSKAEKEK GKTKQEKLKE KVKREKKEKV KMKEKEEVTK AKPACKADKT LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR VPGLTLPSGA FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV EPALCDRLRT QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS SYRKNKWIVE GRLRRLKTVL AKRTGRSEVE MEGPEECLGR RRSSRIMEET SGMEEEEEEE SIAAVPGRRG RRDGEVDATA SSIPELERQI EKLSKRQLFF RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE GNLVPEEVIK KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ EGSPLSLGQS QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA PSQPPEEPEP DEAESSPDPQ ALWFNISAQM PCNAAPTPPP AVSEDQPTPS PQQLASSKPM NRPSAANPCS PVQFSSTPLA GLAPKRRAGD PGEMPQSPTG LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW WIRDPEMLDA MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL AYCEHLSDSQ EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR YLREPLWPTH EVVLEKALLS TPNGAPEGTT TEISYEITPR IRVWRQTLER CRSAAQVCLC LGQLERSIAW EKSVNKVTCL VCRKGDNDEF LLLCDGCDRG CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK RGQKRKSGYS LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG GYTSSEEFAA DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG KQANL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair. Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template. Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex. The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex. Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing.

Gene References into Functions

the results of the present study demonstrated that TIP5 regulates beta-catenin/TCF7L2 signaling via TIP5 during HCC progression and suggests that TIP5 may be a promising therapeutic target for the treatment of HCC. PMID:29620186
Data suggest that binding of helical tail of histone 3 (H3) with PHD ('plant homeodomain') fingers of BAZ2A or BAZ2B (bromodomain adjacent to zinc finger domain 2A or 2B) requires molecular recognition of secondary structure motifs within H3 tail and could represent an additional layer of regulation in epigenetic processes. PMID:28341809
Data show that SUMOylated BANP, E5R, and Nac1 (BEN) domain 3 (BEND3) stabilizes NoRC component TTF-1-interacting protein 5 (Tip5)via association with ubiquitin specific protease 21 (USP21) debiquitinase PMID:26100909
Crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PMID:25533489
The study showed that the NMR structure of the TAM domain of TIP5 resembles the fold of the MBD domain, found in methyl-CpG binding proteins. PMID:25916849
association with ribosomal DNA is impaired in embryonic stem cells and occurs upon cell differentiation PMID:25479748
BAZ2A is overexpressed in prostate cancer, maintains its cell growth, regulates protein-coding genes, and interacts with EZH2 to silence genes repressed in metastasis. Its overexpression is associated with a CpG island methylator phenotype. PMID:25485837
High BAZ2A expression is associated with pancreatic cancer. PMID:25216700
Data show that MOF acetylates TIP5, the largest subunit of NoRC, at a single lysine residue, K633, adjacent to the TIP5 RNA-binding domain, and that SIRT1 (removes the acetyl group from K633. PMID:19578370
the apparent occurrence of an unusual TG 3' splice site in intron 1 is discussed PMID:17672918