Anti-UFM1 antibody [R02-5G1] (STJA0033781)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenA synthetic peptide of human UFM1
STJA0033781
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General Information

Short DescriptionRabbit monoclonal anti-UFM1 for use in WB, IHC-P and IP in Human and Mouse samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB/IHC-P/IP
HostRabbit
ReactivityHuman/Mouse
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDR02-5G1
IsotypeIgG
ConjugationUnconjugated
Concentration0.3 mg/mL
PurificationAffinity Purified
Dilution RangeWB 1:500-1:1000
IHC 1:50-1:100
IP 1:20
Formulation50mM Tris-Glycine (pH 7.4) , 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
Storage InstructionStore at 4°C short term. Aliquot and store at-20°C long term. Avoid freeze/thaw cycles.

Target Information

Gene SymbolUFM1
Gene ID51569
Uniprot IDUFM1_HUMAN
ImmunogenA synthetic peptide of human UFM1

Additional Info

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.
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. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. 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.
Protein Name Ubiquitin-Fold Modifier 1
Database Links
Cellular Localisation Nucleus
Cytoplasm
Alternative Antibody Names Anti-Ubiquitin-Fold Modifier 1 antibody
Anti-UFM1 antibody
Anti-C13orf20 antibody
Anti-BM-002 antibody

Information sourced from Uniprot.org

Citations

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