Expression in Escherichia coli, purification and characterization of LRSAM1, a LRR and RING domain E3 ubiquitin ligase

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Expression in Escherichia coli, purification and characterization of LRSAM1, a LRR and RING domain E3 ubiquitin ligase

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作者：Yanmin Guo¹ ; Weixiang Bian¹ ; Yuan Zhang ; Hongtao Li ; ^{htli@swu.edu.cn" class="auth_mail" title="E-mail the corresponding author}
关键词：LRSAM1 ; Ubiquitin ligase ; RING-finger ; Purification ; Activity
刊名：Protein Expression and Purification
出版年：2017
出版时间：January 2017
年：2017
卷：129
期：Complete
页码：158-161
全文大小：915 K

文摘

class="label">•: LRSAM1 was expressed at high level in Escherichia.coli as inclusion bodies.
class="label">•: LRSAM1 was purified from inclusion bodies through denaturation, renaturation and ammonium sulfate precipitation steps.
class="label">•: The E3 activity of LRSAM1 was pH-dependent in cooperation with UbcH5-type E2-enzymes.
class="label">•: LRSAM1-driven ubiquitination favored K6-, K27-, K29- and K48-linkages.

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