MORF4L2 蛋白, Human (His)

The MORF4L2 protein is an important component of the NuA4 histone acetyltransferase complex and promotes transcriptional activation by acetylating histones H4 and H2A. This modification alters nucleosome-DNA interactions and promotes interactions with other transcription-positive proteins. MORF4L2 Protein, Human (His) is the recombinant human-derived MORF4L2 protein, expressed by E. coli , with C-6*His labeled tag. The total length of MORF4L2 Protein, Human (His) is 288 a.a., with molecular weight of 33-36 kDa.

MORF4L2 蛋白是 NuA4 组蛋白乙酰转移酶复合物的组成部分，通过核小体组蛋白 H4 和 H2A 的乙酰化促进选定基因的转录激活。这种修饰不仅改变了核小体-DNA 相互作用，而且还促进了修饰组蛋白与其他正向调节转录的蛋白质的相互作用。MORF4L2 在 NuA4 复合体中发挥着至关重要的作用，它参与多种细胞过程，包括生长诱导、生长停滞、复制衰老、细胞凋亡和 DNA 修复。RUVBL1 和 RUVBL2 与 EP400 结合，为 NuA4 复合物提供 ATP 酶和解旋酶活性。MORF4L2 也是 MSIN3A 复合体的一个组成部分，该复合体通过核小体组蛋白的脱乙酰化发挥转录抑制作用。在 NuA4 复合体中，MORF4L2 与各种亚基相互作用，包括 KAT5/TIP60、EP400、TRRAP/PAF400 等。此外，MORF4L2 是 MSIN3A 组蛋白脱乙酰酶复合物的一部分，与 SIN3A、HDAC2、ARID4B、MORF4L1、RBBP4/RbAp48 和 RBBP7/RbAp46 合作。它与 MRFAP1 和 RB1 的相互作用，以及与 TLE 转录抑制因子家族的潜在关联，强调了 MORF4L2 在染色质修饰和基因调控中的复杂参与。

Human

E. coli

C-6*His

Q15014 (M1-L288)

9643  [NCBI]

MSSRKQGSQPRGQQSAEEENFKKPTRSNMQRSKMRGASSGKKTAGPQQKNLEPALPGRWGGRSAENPPSGSVRKTRKNKQKTPGNGDGGSTSEAPQPPRKKRARADPTVESEEAFKNRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAILEEYANCKKSQGNVDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILLAHPDAPMSQVYGAPHLLRLFVRIGAMLAYTPLDEKSLALLLGYLHDFLKYLAKNSASLFTASDYKVASAEYHRKAL

33-36 kDa

Greater than 95% as determined by reducing SDS-PAGE.

无菌粉末.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.