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抗人 SENP1 抗体对
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抗人 SENP1 抗体对

01AB00929

SUMO specific peptidase 1 (SENP1) is a cysteine protease that plays essential roles in the SUMO (small ubiquitin-like modifier) pathway. It catalyzes two key functions: processing of SUMO precursors to their mature forms and deconjugation of SUMO from modified proteins. SENP1 is primarily localized in the nucleus and has broad specificity for the three mammalian SUMO paralogs (SUMO-1, SUMO-2, and SUMO-3). The enzyme contains a conserved C-terminal catalytic domain and an N-terminal domain that regulates cellular localization and substrate specificity. SENP1 is crucial for embryonic development and erythropoiesis. Dysregulation of SENP1 has been implicated in various cancers, including prostate cancer, where it enhances androgen receptor-dependent transcription and promotes tumor progression. Additionally, SENP1 has been shown to regulate c-Myc stability and activity, further contributing to its role in cancer development.

Human
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技术参数

靶点基因名
SENP1
蛋白别名
SUMO specific peptidase 1; SENP1
UniProt
Q9P0U3
物种
Human

产品详情

靶点名称
SENP1
蛋白名称
SUMO specific peptidase 1
蛋白别名
Sentrin-specific protease 1; Sentrin/SUMO-specific protease SENP1
靶点基因名
SENP1
UniProt
Q9P0U3
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

SUMO specific peptidase 1 (SENP1) is a cysteine protease that plays essential roles in the SUMO (small ubiquitin-like modifier) pathway. It catalyzes two key functions: processing of SUMO precursors to their mature forms and deconjugation of SUMO from modified proteins. SENP1 is primarily localized in the nucleus and has broad specificity for the three mammalian SUMO paralogs (SUMO-1, SUMO-2, and SUMO-3). The enzyme contains a conserved C-terminal catalytic domain and an N-terminal domain that regulates cellular localization and substrate specificity. SENP1 is crucial for embryonic development and erythropoiesis. Dysregulation of SENP1 has been implicated in various cancers, including prostate cancer, where it enhances androgen receptor-dependent transcription and promotes tumor progression. Additionally, SENP1 has been shown to regulate c-Myc stability and activity, further contributing to its role in cancer development.