MSL3 (基因名), Male-specific lethal 3 homolog (蛋白名), MS3L1_HUMAN.
Human MSL3/ Male-specific lethal 3 homolog Recombinant Protein
Male-specific lethal-3 homolog 1, Male-specific lethal-3 protein-like 1, MSL3-like 1, MSL3L1
>90% by SDS-PAGE
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50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole, 10%glycerol(PH8.0)
Store at -20°C. (Avoid repeated freezing and thawing.)
Component the MSL histone acetyltransferase complex at least composed of the MOF/KAT8, MSL1/hampin, MSL2 and MSL3. Interacts (via the MRG domain) with MSL1.
May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.
MSASEGMKFK | FHSGEKVLCF | EPDPTKARVL | YDAKIVDVIV | GKDEKGRKIP |
EYLIHFNGWN | RSWDRWAAED | HVLRDTDENR | RLQRKLARKA | VARLRSTGRK |
KKRCRLPGVD | SVLKGLPTEE | KDENDENSLS | SSSDCSENKD | EEISEESDIE |
EKTEVKEEPE | LQTRREMEER | TITIEIPEVL | KKQLEDDCYY | INRRKRLVKL |
PCQTNIITIL | ESYVKHFAIN | AAFSANERPR | HHHVMPHANM | NVHYIPAEKN |
VDLCKEMVDG | LRITFDYTLP | LVLLYPYEQA | QYKKVTSSKF | FLPIKESATS |
TNRSQEELSP | SPPLLNPSTP | QSTESQPTTG | EPATPKRRKA | EPEALQSLRR |
STRHSANCDR | LSESSASPQP | KRRQQDTSAS | MPKLFLHLEK | KTPVHSRSSS |
PIPLTPSKEG | SAVFAGFEGR | RTNEINEVLS | WKLVPDNYPP | GDQPPPPSYI |
YGAQHLLRLF | VKLPEILGKM | SFSEKNLKAL | LKHFDLFLRF | LAEYHDDFFP |
ESAYVAACEA | HYSTKNPRAI | Y
"Characterization of a novel chromo domain gene in xp22.3 with homology to Drosophila msl-3."
"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
"Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain."
"Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4."
"A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
"Origin and evolution of the regulatory gene male-specific lethal-3."
"Architecture of the human interactome defines protein communities and disease networks."
"Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes."
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