SAE1 Human

SUMO1 Activating Enzyme Subunit 1 Human Recombinant
Cat. No.
BT16753
Source
Escherichia Coli.
Synonyms
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

SAE1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (1-346 a.a.) and having a molecular mass of 42.2 kDa. The SAE1 is fused to 32 amino acid T7-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
SAE1, a member of the ubiquitin-activating E1 protein family, plays a crucial role in the initial step of the UBL1 conjugation pathway. This pathway tags proteins with ubiquitin (Ub) for subsequent degradation by the 26S Proteasome. As a UBLI E1 ligase, SAE1 facilitates the ATP-dependent activation of UBL1. It forms a heterodimer with UBLE1A and UBLE1B, enabling the complex to bind UBL1. SAE1, a dimeric enzyme, functions as an E1 ligase for SUMO1, SUMO2, SUMO3, and potentially SUMO4. It regulates the ATP-dependent activation of SUMO proteins and the formation of a thioester bond with a conserved cysteine residue on SAE2.
Description
Recombinant Human SAE1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 378 amino acids (residues 1-346). With a molecular weight of 42.2 kDa, this SAE1 protein is fused to a 32 amino acid T7-Tag at its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
SAE1 Human solution is prepared in a buffer consisting of 20mM Tris pH 8.0, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Minimize repeated freeze-thaw cycles.
Purity
Purity exceeds 90.0% as determined by SDS-PAGE analysis.
Synonyms
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
Source
Escherichia Coli.
Amino Acid Sequence
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMVEKEEAG GGISEEEAAQ YDRQIRLWGL EAQKRLRASR VLLVGLKGLG AEIAKNLILA GVKGLTMLDH EQVTPEDPGA QFLIRTGSVG RNRAEASLER AQNLNPMVDV KVDTEDIEKK PESFFTQFDA VCLTCCSRDV IVKVDQICHK NSIKFFTGDV FGYHGYTFAN LGEHEFVEEK TKVAKVSQGV EDGPDTKRAK LDSSETTMVK KKVVFCPVKE ALEVDWSSEK AKAALKRTTS DYFLLQVLLK FRTDKGRDPS SDTYEEDSEL LLQIRNDVLD SLGISPDLLP EDFVRYCFSE MAPVCAVVGG ILAQEIVKAL SQRDPPHNNF FFFDGMKGNG IVECLGPK.

Product Science Overview

Introduction

SUMO1 Activating Enzyme Subunit 1 (SAE1) is a crucial component in the process of SUMOylation, a post-translational modification that involves the attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins. This modification plays a significant role in various cellular processes, including nuclear-cytosolic transport, transcriptional regulation, apoptosis, and protein stability.

Structure and Function

SAE1, along with SAE2, forms the heterodimeric enzyme complex known as the SUMO-activating enzyme (E1). This complex is responsible for the activation of SUMO proteins, a critical first step in the SUMOylation pathway. The activation process involves the ATP-dependent adenylation of the SUMO C-terminus, followed by the formation of a thioester bond between the SUMO and the catalytic cysteine of SAE2 .

Biological Significance

SUMOylation is essential for maintaining cellular homeostasis and responding to stress. It regulates various cellular functions by modifying the activity, stability, and localization of target proteins. In particular, SAE1 has been implicated in the regulation of transcription factors, DNA repair proteins, and other key regulatory proteins .

Clinical Relevance

The dysregulation of SUMOylation, including the activity of SAE1, has been associated with several diseases, including cancer. For instance, in breast cancer, alterations in the SUMOylation pathway can influence tumor progression and metastasis . SAE1 has been identified as a potential biomarker for the prognosis of triple-negative breast cancer (TNBC), one of the most aggressive subtypes of breast cancer .

Research and Therapeutic Potential

Given its pivotal role in SUMOylation, SAE1 is a target of interest for therapeutic interventions. Inhibitors of the SUMOylation pathway are being explored as potential treatments for cancers and other diseases characterized by aberrant SUMOylation . Additionally, recombinant SAE1 proteins are used in research to study the mechanisms of SUMOylation and to develop SUMOylation-based assays.

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