UFC1 Human

Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
Cat. No.
BT20352
Source
Escherichia Coli.
Synonyms

Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks 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

UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.
UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
UFC1, a member of the ubiquitin-conjugating enzyme family, acts as an E2-like conjugating enzyme for ubiquitin-fold modifier-1 (UFM1). The process involves UBA5, a novel E1-like enzyme, activating UFM1 by forming a high-energy thioester bond. Subsequently, activated UFM1 is transferred to UFC1, its corresponding E2-like enzyme, through a similar thioester linkage.
Description
Produced in E.Coli, UFC1 is a single, non-glycosylated polypeptide chain consisting of 187 amino acids (specifically, amino acids 1 to 167) and possesses a molecular mass of 21.6kDa. This UFC1 protein is fused to a 20 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized through filtration.
Formulation
This solution contains 1mg/ml of UFC1 protein and is prepared in a buffer consisting of 20mM Tris-HCl (pH 8.0), 20% glycerol, 0.1M NaCl, and 1mM DTT.
Stability
While UFC1 Human Recombinant exhibits stability at 4°C for a week, it is recommended to store it below -18°C to ensure its long-term integrity. It's essential to avoid repeated freeze-thaw cycles.
Purity
SDS-PAGE analysis confirms a purity exceeding 90%.
Synonyms

Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.

Product Science Overview

Introduction

Ubiquitin Fold Modifier Conjugating Enzyme 1 (UFC1) is a crucial component in the ubiquitin-like modification system known as ufmylation. This system is essential for various cellular processes, including protein degradation, signal transduction, and cellular stress responses. UFC1 is a human recombinant protein that plays a pivotal role in the conjugation of Ubiquitin-Fold Modifier 1 (UFM1) to target proteins.

Gene and Protein Structure

The UFC1 gene is located on chromosome 1 and encodes a protein that is part of the E2 enzyme family. The UFC1 protein is responsible for the second step in the ufmylation pathway, where it accepts UFM1 from the E1 enzyme UBA5 and forms a thioester linkage with UFM1 . This process is crucial for the subsequent transfer of UFM1 to target proteins, mediated by E3 ligases.

Biological Functions

UFC1 and the ufmylation system are involved in several critical cellular functions:

  • Protein Quality Control: Ufmylation helps in the degradation of misfolded proteins, maintaining cellular homeostasis.
  • Endoplasmic Reticulum (ER) Stress Response: Ufmylation is involved in reticulophagy, a process that removes damaged ER, thus alleviating ER stress .
  • Erythroid Development: The ufmylation system, including UFC1, is essential for the proper development of erythroid cells, which are precursors to red blood cells .
Clinical Significance

Mutations or dysregulation of UFC1 and the ufmylation pathway have been associated with various diseases:

  • Neurodevelopmental Disorders: Mutations in UFC1 can lead to neurodevelopmental disorders characterized by spasticity and poor growth .
  • Osteoarthritis: Alterations in the ufmylation pathway have been linked to the development of osteoarthritis .
Research and Therapeutic Potential

The study of UFC1 and the ufmylation system is ongoing, with researchers exploring its potential therapeutic applications:

  • Cancer: Ufmylation has been implicated in tumorigenesis, and targeting this pathway could offer new cancer treatment strategies .
  • Blood Disorders: Modulating ufmylation activity may provide novel approaches to treat blood-related diseases such as anemia .

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