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Product
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BRD4 (49-460aa), His, Human
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Cat#
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101-32-106A
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Sequence
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MHHHHHHETS NPNKPKRQTN QLQYLLRVVL KTLWKHQFAW
PFQQPVDAVK LNLPDYYKII KTPMDMGTIK KRLENNYYWN
AQECIQDFNT MFTNCYIYNK PGDDIVLMAE ALEKLFLQKI
NELPTEETEI MIVQAKGRGR GRKETGTAKP GVSTVPNTTQ
ASTPPQTQTP QPNPPPVQAT PHPFPAVTPD LIVQTPVMTV
VPPQPLQTPP PVPPQPQPPP APAPQPVQSH PPIIAATPQP
VKTKKGVKRK ADTTTPTTID PIHEPPSLPP EPKTTKLGQR
RESSRPVKPP KKDVPDSQQH PAPEKSSKVS EQLKCCSGIL
KEMFAKKHAA YAWPFYKPVD VEALGLHDYC DIIKHPMDMS
TIKSKLEARE YRDAQEFGAD VRLMFSNCYK YNPPDHEVVA
MARKLQDVFE MRFAKMPDE
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Unit/Weight
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100 μg
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Unit Price
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$188.00
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Description
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Bromodomain (BRD) is an extensive family of protein domains, originally identified in and named after the Drosophila protein Brahma. Members of BRD family share a conserved atypical left-handed four helix bundle structure, and specifically bind to ε-lysine acetylated proteins. It is well known that histone acetylation and methylation play a central role in epigenetics and are important for various gene transcription events, thus the acetyl-lysine binding property of BRDs make them suitable drug targets for epigenetics. Currently, there are 46 diverse human proteins containing 61 BRDs. These include histone acetyltransferases, ATP-dependent chromatin-remodeling complex proteins, and nuclear scaffold proteins. The main functions of BRDs in vivo include chromatin acetylation and deacetylation, nucleosome assembly and remodeling, and organizations of chromosome or chromatin domains.
Recombinant human BRD4 (49-460) with His tag produced in E.coli is a single, non-glycosylated polypeptide chain containing 419 amino acids. A fully biologically active molecule, BRD4 (49-460) has a molecular mass of 47.5 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at Pepmic.
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Molecular Weight
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47.5 kDa, observed by reducing SDS-PAGE.
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Purity
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> 95% by SDS-PAGE and HPLC analysis.
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Storage
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BRD4 (49-460) remains stable up to 6 months at -80℃ from date of receipt. For maximum recovery of product, centrifuge original vial prior to removing the cap. Aliquot to avoid repeated thawing and freezing.
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