Recombinant A. thaliana Ubiquitin

Name: Recombinant A. thaliana Ubiquitin
SKU: DAG2657
Rating: 5 (1 reviews)

A. thaliana Ubiquitin, recombinant protein from E. coli

COA

SDS

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Summary

Product Overview

Recombinant Plant Ubiquitin

Nature

Recombinant

Tag/Conjugate

Unconjugated

Purity

> 95% by SDS-PAGE

Format

5 mg, lyophilized powder

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Similarity: Belongs to the ubiquitin family. Contains 3 ubiquitin-like domains.

Keywords

FLJ25987; MGC8385; Polyubiquitin B; RPS 27A; RPS27A; UBA 52; UBA 80; UBA52; UBA80; UBB; UBB; UBC; UBCEP 1; UBCEP 2; UBCEP1; UBCEP2; Ubiquitin; ubiquitin B;

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References

Overexpression ofCpSIZ1, a SIZ/PIAS-Type SUMO E3 Ligase from Wintersweet (Chimonanthus praecox), Delays Flowering, Accelerates Leaf Senescence and Enhances Cold Tolerance in Arabidopsis

PLANT MOLECULAR BIOLOGY REPORTER

Authors: Li, Rui; Ma, Jing; Liu, Huamin; Wang, Xia; Li, Jing; Li, Zhineng; Li, Mingyang; Sui, Shunzhao; Liu, Daofeng

Abstract

Wintersweet (Chimonanthus praecoxL.) is a traditional winter-flowering plant in China and a popular cut flower in winter. Its unique flowering characteristics under cold stress may involve the regulation of a large number of proteins. Protein post-translational modification is an important regulating type for the gene function. However, little is known about the post-translational modification in wintersweet. SUMOylation is an important post-translational modification in eukaryotes. Small ubiquitin-like modifier (SUMO) E3 ligases perform multiple functional regulatory activities in plants via SUMOylation. Here, we cloned and identified a SIZ/PIAS-type SUMO E3 ligase,CpSIZ1, from wintersweet.CpSIZ1shared high similarity with other SIZ1 proteins. Quantitative real-time PCR (qRT-PCR) indicated thatCpSIZ1was expressed in all tissues tested, with the highest expression in flower wither period of stage 6, and followed by mature leaves except for different flower development stages. The ectopic expression ofCpSIZ1in Arabidopsis, including theCpSIZ1overexpression insiz1-2mutant (HB line) andCpSIZ1overexpression in WT (OE line), not only promoted vegetative growth, delayed flowering and accelerated leaf senescence, but also improve the cold tolerance in Arabidopsis. Therefore, our studies have enrich the understanding of function ofSIZ1gene in woody plant, and provide a good foundation for further research on the post-translational modification regulation mechanism in this winter-flowering plant.

Circulating glial fibrillary acidic protein and ubiquitin carboxy-terminal hydrolase-L1 as markers of neuronal damage in children with epileptic seizures

CHILDS NERVOUS SYSTEM

Authors: Elhady, Marwa; Youness, Eman R.; AbuShady, Mones M.; Nassar, Maysa S.; Elaziz, Ali Abd; Masoud, Mahmoud M.; Foudaa, Fayez K.; Abu Elhamed, Walaa Alshasrany

Abstract

Background Epilepsy is a common neurological disease that has a negative impact on physical, social, and cognitive function. Seizure-induced neuronal injury is one of the suggested mechanisms of epilepsy complications. We aimed to evaluate the circulating level of glial fibrillary acidic protein (GFAP) and ubiquitin carboxy-terminal hydrolase-L1 (UCH-L1) as markers of neuronal damage in children with epilepsy and its relation to epilepsy characteristics. Study designMethods This case control study included 30 children with epilepsy and 30 healthy children as a control group. Seizure severity was determined based on Chalfont score. Serum level of GFAP and UCH-L1were measured, and their associations with epilepsy characteristics were investigated. Results Circulating levels of GFAP and UCH-L1 were significantly higher in children with epilepsy than in controls (17.440 +/- 6.74 and 5.700 +/- 1.64 vs 7.06 +/- 3.30 and 1.81 +/- 0.23, respectively) especially in those with generalized and active seizures. GFAP and UCH-L1 were significantly correlated to the severity of seizures in the previous 6 months. Elevated GFAP level was a predictor for active seizures (OR 1.841, 95%CI 1.043-3.250,P = 0.035). Conclusion Circulating GFAP and UCH-L1 expression is increased in children with epilepsy especially those with active seizures. Significance GFAP and UCH-L 1may serve as peripheral biomarkers for neuronal damage in children with epilepsy that can be used to monitor disease progression and severity for early identification of those with drug-resistant epilepsy and those who are in need for epilepsy surgery.