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AB104461

Recombinant Human UFM1 protein

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Recombinant Human UFM1 protein is a Human Full Length protein, in the 1 to 83 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

C13orf20, BM-002, UFM1, Ubiquitin-fold modifier 1

1 Images
SDS-PAGE - Recombinant Human UFM1 protein (AB104461)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human UFM1 protein (AB104461)

15% SDS-PAGE showing ab104461 (3 μg) at approximately 11.1 kDa.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P61960

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSKVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRIIPRDRVG","proteinLength":"Full Length","predictedMolecularWeight":"11.1 kDa","actualMolecularWeight":null,"aminoAcidEnd":83,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P61960","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

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
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.

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.

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

Product protocols

Target data

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).
See full target information UFM1

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