类泛素蛋白1重组兔单抗

Rrmab®兔单抗
2026-01-04~2026-02-28,RR26012026-01-04~2026-02-28,TR
类泛素蛋白1重组兔单抗
货号:bsm-61144R
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概述

产品编号
bsm-61144R
产品类型
重组兔单抗
英文名称
SUMO1 Recombinant Rabbit mAb
中文名称
类泛素蛋白1重组兔单抗
英文别名
DAP1; GMP1; OFC10; PIC1; SENP2; SMT3; SMT3C; SMT3H3; UBL1; SENTRIN; SMTP3; SUMO-1; SUMO1_HUMAN; SUMO1; GAP-modifying protein 1 (GMP1); SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein SMT3C (Smt3C); Ubiquitin-like protein UBL1; SUMO1_MOUSE; SUMO1_RAT;
抗体来源
Rabbit
免疫原
A synthesized peptide derived from human Sumo 1: 70-101
亚型
IgG
性状
Liquid
纯化方法
affinity purified by Protein A
克隆类型
Recombinant
克隆号
5F3
理论分子量
12
检测分子量
12
储存液
10mM phosphate buffered saline(pH 7.4) with 150mM sodium chloride, 0.05% BSA, 0.02% Proclin300 and 50% glycerol.
SWISS
Gene ID
保存条件
Store at 4℃ for short term. Store at -20℃ for long term. Avoid repeated freeze/thaw cycles.
注意事项
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
产品介绍
合成与降解(Synthesis and Degradation)
SUMO化能够使蛋白质更加稳定,SUMO的生化反应途径与泛素相似,但不像泛素那样诱导底物蛋白降解.进而调节许多关键的细胞活动. SUMO(small ubiquitin-related modifier)是泛素(ubiqutin)类蛋白家族的重要成员之一.
背景资料
SUMO1 Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction.
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产品应用

应用已检合格种属预测种属推荐稀释比例
WBHuman, Mouse, Rat1:500-2000
IHC-PHuman, Mouse, Rat1:100-500
IHC-FHuman, Mouse, Rat1:100-500
IFHuman, Mouse, Rat1:100-500
Flow-CytHuman, Mouse, Rat1:50-100
ICC/IFHumanMouse, Rat1:50-200
IPHuman, Mouse, Rat1:20-50

交叉反应

交叉反应: Human, Mouse, Rat

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靶标

基因名
SUMO1
蛋白名
Small ubiquitin-related modifier 1
亚基
Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25.
亚细胞定位
Nucleus membrane. Nucleus speckle. Cytoplasm. Note=Recruited by BCL11A into the nuclear body.
翻译后修饰
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
疾病
Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:613705]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.
相似性
Belongs to the ubiquitin family. SUMO subfamily.
Contains 1 ubiquitin-like domain.
功能
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.

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