UBA2 Human

Ubiquitin-Like Modifier Activating Enzyme 2 Human Recombinant
Cat. No.
BT16979
Source
Sf9, Baculovirus cells.
Synonyms

SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 2.

Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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.
Shipped with Ice Packs
In Stock

Description

UBA2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 649 amino acids (1-640a.a) and having a molecular mass of 72.3kDa. UBA2 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
SUMO-activating enzyme subunit 2 (UBA2) is a member of a family of small, related proteins that can be enzymatically attached to a target protein through a post-translational modification process known as sumoylation. UBA2 is conjugated to various molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme. UBA2 plays a critical role in protecting neurons during periods of cerebral ischemia.
Description
Recombinant Human UBA2, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 649 amino acids (1-640a.a.) with a molecular mass of 72.3 kDa. UBA2 is fused to a 6 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
UBA2 protein solution at a concentration of 0.5 mg/ml in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For longer storage periods, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity greater than 85.0% as determined by SDS-PAGE analysis.
Synonyms

SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 2.

Source
Sf9, Baculovirus cells.
Amino Acid Sequence
ADLMALSRGL PRELAEAVAG GRVLVVGAGG IGCELLKNLV LTGFSHIDLI DLDTIDVSNL NRQFLFQKKH VGRSKAQVAK ESVLQFYPKA NIVAYHDSIM NPDYNVEFFR QFILVMNALD NRAARNHVNR MCLAADVPLI ESGTAGYLGQ VTTIKKGVTE CYECHPKPTQ RTFPGCTIRN TPSEPIHCIV WAKYLFNQLF GEEDADQEVS PDRADPEAAW EPTEAEARAR ASNEDGDIKR ISTKEWAKST GYDPVKLFTK LFKDDIRYLL TMDKLWRKRK PPVPLDWAEV QSQGEETNAS DQQNEPQLGL KDQQVLDVKS YARLFSKSIE TLRVHLAEKG DGAELIWDKD DPSAMDFVTS AANLRMHIFS MNMKSRFDIK SMAGNIIPAI ATTNAVIAGL IVLEGLKILS GKIDQCRTIF LNKQPNPRKK LLVPCALDPP NPNCYVCASK PEVTVRLNVH KVTVLTLQDK IVKEKFAMVA PDVQIEDGKG TILISSEEGE TEANNHKKLS EFGIRNGSRL QADDFLQDYT LLINILHSED LGKDVEFEVV GDAPEKVGPK QAEDAAKSIT NGSDDGAQPS TSTAQEQDDV LIVDSDEEDS SNNADVSEEE RSRKRKLDEK ENLSAKRSRI EQKEELDDVI ALDHHHHHH

Product Science Overview

Introduction

Ubiquitin-Like Modifier Activating Enzyme 2 (UBA2), also known as SUMO-activating enzyme subunit 2 (SAE2), is a crucial component in the post-translational modification process known as SUMOylation. This process involves the attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins, influencing various cellular functions such as signal transduction, gene expression, and protein stability.

Historical Background

The concept of ubiquitin-like protein modification was first characterized in the early 1980s. UBA2 was initially identified during the characterization of E1 enzymatic activity in wheat. Human UBA2, which contains 640 amino acid residues, shares a high degree of sequence identity with SAE1, despite the latter being only 346 amino acids long. Together, these proteins form a functional heterodimeric enzyme that activates SUMO proteins in a manner analogous to the single E1 ubiquitin-activating enzymes in yeast .

Structure and Function

UBA2 is a subunit of the E1-activating enzyme involved in the SUMOylation of numerous proteins. It forms a heterodimer with SAE1, and this complex is responsible for the ATP-dependent activation of SUMO proteins. The activated SUMO is then transferred to a conjugating enzyme (E2), which, with the assistance of an E3 ligase, attaches the SUMO to the target protein .

Biological Significance

SUMOylation plays a vital role in various cellular processes, including cell cycle control, apoptosis, cell differentiation, and the stress response. UBA2, as part of the SUMO-activating enzyme, is essential for these processes. The modification of proteins by SUMO can alter their structure, localization, and interaction with other proteins, thereby regulating their function .

Clinical Relevance

UBA2 has been implicated in the progression of various cancers. For instance, it has been observed that UBA2 is overexpressed in glioma tissues and cell lines. High expression levels of UBA2 are associated with poorer survival rates in glioma patients. Additionally, UBA2 expression correlates with drug sensitivity in cancers, making it a potential therapeutic target .

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