Recombinant Human UFM1 protein is a Human Full Length protein, in the 1 to 83 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Key facts
- Purity
>95% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE, MS
- Biologically active
No
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M S K V S F K I T L T S D P R L P Y K V L S V P E S T P F T A V L K F A A E E F K V P A A T S A I I T N D G I G I N P A Q T A G N V F L K H G S E L R I I P R D R V G
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776, PubMed:30626644, PubMed:38377992, PubMed:38383785). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776). Ufmylation is involved in various processes, such as ribosome recycling, response to DNA damage, transcription or reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:25219498, PubMed:32160526, PubMed:38383785).
Alternative names
C13orf20, BM-002, UFM1, Ubiquitin-fold modifier 1
Recommended products
Recombinant Human UFM1 protein is a Human Full Length protein, in the 1 to 83 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
Key facts
- Purity
>95% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE, MS
- Biologically active
No
- Accession
- P61960-1
- Animal free
No
- Species
Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl
Sequence info
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M S K V S F K I T L T S D P R L P Y K V L S V P E S T P F T A V L K F A A E E F K V P A A T S A I I T N D G I G I N P A Q T A G N V F L K H G S E L R I I P R D R V G
- Accession
- P61960
- Protein length
Full Length
- Predicted molecular weight
11.1 kDa
- Amino acids
1 to 83
- Nature
Recombinant
- Tags
His tag N-Terminus
Specifications
- Form
Liquid
- Additional notes
ab104461 is purified using conventional chromatography techniques.
General info
- Function
Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776, PubMed:30626644, PubMed:38377992, PubMed:38383785). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:27653677, PubMed:29868776). Ufmylation is involved in various processes, such as ribosome recycling, response to DNA damage, transcription or reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:25219498, PubMed:32160526, PubMed:38383785).
- Sequence similarities
Belongs to the UFM1 family.
- Post-translational modifications
UFM1 precursor is cleaved by UFSP1, promoting its maturation: processing of the C-terminal Ser-Cys dipeptide is required to expose its C-terminal conserved Gly residue.
- Subcellular localisation
Nucleus
Storage
- Shipped at conditions
Blue Ice
- Appropriate short-term storage conditions
-20°C
- Appropriate long-term storage conditions
-20°C
- Aliquoting information
Upon delivery aliquot
- Storage information
Avoid freeze / thaw cycle
Supplementary info
This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
UFM1 also called ubiquitin-fold modifier 1 is a small protein modifier with a mass of approximately 9 kDa. It is part of the ubiquitin-like protein family and primarily expressed in a wide range of tissues. UFM1 is involved in a unique form of post-translational modification known as UFMylation where it conjugates to substrate proteins altering their function and stability. This process plays a role in regulating cell cycle and apoptosis among other cellular processes.
- Biological function summary
UFM1 functions as a signaling molecule that influences various cellular pathways. It acts as part of a complex with other enzymes including UBA5 UFC1 and UFL1 which are important for its conjugation process. This modification system plays a role in endoplasmic reticulum (ER) stress response by affecting proteins involved in ER-associated degradation (ERAD). Its interaction with these proteins helps cells manage stress and maintain homeostasis.
- Pathways
UFM1 participates in the ER stress response pathway and is also connected to the mTOR signaling pathway. Both pathways are essential for cell growth and survival. Within these pathways UFM1 interacts with proteins like mLST8 in the mTOR pathway integrating signals that coordinate cell metabolism growth and apoptosis. The precise regulation of these pathways highlights UFM1's role in maintaining cellular equilibrium.
- Associated diseases and disorders
UFM1 has been linked to cancer and congenital disorders. Altered UFMylation due to mutations in related genes can contribute to tumor development by affecting protein degradation and cellular stress responses. In hereditary conditions dysfunctional UFM1 activity can lead to rare disorders affecting metabolism and neurological function. Proteins like mLST8 which interact with UFM1 in pathways can also play a role in these disease mechanisms suggesting potential targets for therapeutic intervention.
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1 product image
SDS-PAGE - Recombinant Human UFM1 protein (ab104461)
15% SDS-PAGE showing ab104461 (3 μg) at approximately 11.1 kDa.
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