UFM1 Human

Ubiquitin-Fold Modifier 1 Human Recombinant
Cat. No.
BT23053
Source
Escherichia Coli.
Synonyms
Ubiquitin-fold modifier 1, UFM1, C13orf20, BM-002, bA131P10.1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

UFM1 Human Recombinant fused with a20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing103 amino acids (1-83 a.a) and having a molecular mass of 11.1kDa. The UFM1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
UFM1, a ubiquitin-like protein, undergoes conjugation with target proteins via a ubiquitylation-like process. This involves the E1-like activating enzyme UBA5 and the E2-like conjugating enzyme UFC1. While primarily localized in the nucleus, UFM1 is also found diffusely in the cytoplasm and is expressed in various tissues such as the kidney, brain, heart, liver, and lung.
Description
Recombinant human UFM1, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This non-glycosylated polypeptide chain consists of 103 amino acids (1-83 a.a), resulting in a molecular mass of 11.1 kDa. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The UFM1 solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris (pH 8.0) and 10% glycerol.
Stability
For optimal storage, refrigerate at 4°C if the entire vial will be used within 2-4 weeks. For longer-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as assessed by SDS-PAGE.
Synonyms
Ubiquitin-fold modifier 1, UFM1, C13orf20, BM-002, bA131P10.1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVG.

Product Science Overview

Introduction

Ubiquitin-Fold Modifier 1 (UFM1) is a ubiquitin-like protein that plays a crucial role in various cellular processes. It is a small protein consisting of 85 amino acids and is highly conserved across multicellular organisms . UFM1 is involved in a post-translational modification process known as ufmylation, which is analogous to ubiquitination.

Structure and Expression

UFM1 is synthesized as a precursor protein (pro-UFM1) and undergoes processing to become the mature form. The mature UFM1 can be covalently attached to target proteins via an isopeptide bond to lysine residues . This attachment can occur as a monomer or as a lysine-linked polymer . The recombinant form of UFM1 is typically expressed in Escherichia coli and purified to high levels of purity (>95%) for research purposes .

Ufmylation Process

The ufmylation process involves several key enzymes:

  1. UFM1-activating enzyme (UBA5): This enzyme activates UFM1 in an ATP-dependent manner.
  2. UFM1-conjugating enzyme (UFC1): This enzyme transfers the activated UFM1 to the target protein.
  3. UFM1-ligase (UFL1): This enzyme facilitates the attachment of UFM1 to the substrate protein .
Biological Functions

Ufmylation is implicated in various cellular functions, including:

  • Endoplasmic Reticulum (ER) Stress Response: Ufmylation is involved in reticulophagy (ER-phagy), a process that helps cells cope with ER stress .
  • Transcription Regulation: Ufmylation of TRIP4 regulates nuclear receptor-mediated transcription .
  • Protein Quality Control: Ufmylation plays a role in maintaining protein homeostasis by targeting misfolded proteins for degradation .
Clinical Significance

Mutations or dysregulation of the UFM1 pathway have been associated with several diseases, including:

  • Leukodystrophy, Hypomyelinating, 14: A genetic disorder characterized by abnormal development of the white matter in the brain .
  • Leukodystrophy, Hypomyelinating, 6: Another genetic disorder affecting the myelin sheath of nerve cells .
Research Applications

Recombinant UFM1 is widely used in research to study the mechanisms of ufmylation and its role in various cellular processes. It is also used to investigate the potential therapeutic targets for diseases associated with UFM1 dysregulation .

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