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Product
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BRD3 (29-145aa), His, Human
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Cat#
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101-32-105A
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Sequence
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MHHHHHHEVS NPKKPGRVTN QLQYLHKVVM KALWKHQFAW
PFRQPVDAVK LGLPDYHKII KQPMDMGTIK RRLENNYYWA
ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ TLEKIFLQKV
ASMPQEEQEL VVTIPKNSHK KGAKLAALQG SVTSAHQVPA
VSSVSHTALY TPPPEIPTTV LNIPHPSVIS SPLLKSLHSA
GPPLLAVTAA PPAQPLAKKK GVKRKADTTT PTPTAILAPG
SPASPPGSLE PKAARLPPMR RESGRPIKPP RKDLPDSQQQ
HQSSKKGKLS EQLKHCNGIL KELLSKKHAA YAWPFYKPVD
ASALGLHDYH DIIKHPMDLS TVKRKMENRD YRDAQEFAAD
VRLMFSNCYK YNPPDHDVVA MARKLQDVFE FRYAKMPDEP
LE
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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 BRD2 (65-459) with His tag produced in E. coli is a single, non-glycosylated polypeptide chain containing 402 amino acids. A fully biologically active molecule, BRD2 (65-459) has a molecular mass of 45.3 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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45.3 kDa, observed by reducing SDS-PAGE.
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Purity
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> 95% by reducing SDS-PAGE.
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Storage
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BRD2 (65-459) 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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