Anti-Recombinant-SMYD3 antibody [RM2L71] (STJA0026035)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
STJA0026035
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General Information

Short DescriptionRabbit monoclonal anti-Recombinant-Histone-Lysine N-Methyltransferase Smyd3 for use in FC, IF, IHC, IP and WB in Human, Mouse and Rat samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsFC/IF/IHC/IP/WB
HostRabbit
ReactivityHuman/Mouse/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDRM2L71
IsotypeIgG
ConjugationUnconjugated
PurificationProtein A/G purified from cell culture supernatant
Dilution RangeFCM: 1:20-1:100, IF: 1:50-1:200, IHC: 1:100-1:200, IP: 1:20-1:50, WB: 1:1000-1:2000
Formulation0.01M PBS, pH 7.4, 0.05% BSA, 50% Glycerol, 0.05% Sodium Azide
Storage InstructionSuitable for storage at +4°C between 1-2 weeks. For longer term store at-20°C for up to 12 months.

Target Information

Gene SymbolSMYD3
Gene ID64754
Uniprot IDSMYD3_HUMAN

Additional Info

Function Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.
Protein Name Histone-Lysine N-Methyltransferase Smyd3
Set And Mynd Domain-Containing Protein 3
Zinc Finger Mynd Domain-Containing Protein 1
Database Links Reactome: R-HSA-3214841
Cellular Localisation Cytoplasm
Nucleus
Mainly Cytoplasmic When Cells Are Arrested At G0/G1
Accumulates In The Nucleus At S Phase And G2/M
Alternative Antibody Names Anti-Histone-Lysine N-Methyltransferase Smyd3 antibody
Anti-Set And Mynd Domain-Containing Protein 3 antibody
Anti-Zinc Finger Mynd Domain-Containing Protein 1 antibody
Anti-SMYD3 antibody
Anti-ZMYND1 antibody
Anti-ZNFN3A1 antibody

Information sourced from Uniprot.org

Citations

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