UBA5 Human

Ubiquitin-Like Modifier Activating Enzyme 5 Human Recombinant
Cat. No.
BT17159
Source
Escherichia Coli.
Synonyms
Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

UBA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4kDa.
UBA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of the ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates a ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in the cytoplasm, while it generally localizes to the nucleus in the presence of SUMO2.
Description
Recombinant human UBA5 produced in E. coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4 kDa. UBA5 is fused to a 24 amino acid His-tag at the N-terminus and purified by proprietary chromatographic techniques.
Physical Appearance
Colorless, sterile-filtered solution.
Formulation
The UBA5 solution (0.5 mg/ml) is supplied in 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 10% glycerol, and 50 mM NaCl.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, store at -20°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Greater than 90.0% purity as determined by SDS-PAGE.
Synonyms
Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN
FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH
EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM.

Product Science Overview

Gene and Protein Structure

The UBA5 gene is located on chromosome 3 (3q22.1) and spans approximately 25,348 base pairs . The gene produces multiple transcript variants through alternative splicing, resulting in distinct isoforms of the protein . The primary structure of UBA5 consists of 404 amino acids .

Function and Mechanism

UBA5 specifically catalyzes the first step in the ufmylation pathway, which involves the activation of ubiquitin-fold modifier 1 (UFM1) . This process begins with the adenylation of the C-terminal glycine residue of UFM1 using ATP. Subsequently, this residue is linked to the side chain of a cysteine residue in UBA5, forming a high-energy thioester bond and releasing AMP . This activation is essential for the subsequent transfer of UFM1 to its target proteins.

Biological Significance

The ufmylation pathway, mediated by UBA5, is involved in various cellular processes, including protein quality control, response to endoplasmic reticulum stress, and regulation of intracellular signaling pathways . Dysregulation of UBA5 has been associated with several diseases, such as spinocerebellar ataxia, autosomal recessive 24, and developmental and epileptic encephalopathy 44 .

Research and Applications

Human recombinant UBA5 is widely used in research to study the ufmylation pathway and its implications in health and disease. By understanding the role of UBA5 in cellular processes, researchers aim to develop therapeutic strategies for conditions associated with its dysfunction .

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