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Western blot(SDS PAGE) analysis of extracts from HEK-293 cells.Using KMT1B / SUV39H2Rabbit mAb [K693] at dilution of 1:1000 incubated at 4℃ over night.
Protein names :SUV39H2,KMT1B,SUV92_HUMAN,Histone-lysine N-methyltransferase SUV39H2 3-9 homolog 2)
UniProtID :Q9H5I1
MASS(da) :46,682
MW(kDa) :47,54 kDa
Form :Liquid
Purification :Protein A purification
Host :Rabbit
Isotype :IgG
sensitivity :Endogenous
Reactivity :Human,Mouse,Rat
Specificity :Antibody is produced by immunizing animals with a synthetic peptide at the sequence of human KMT1B / SUV39H2
Storage :Antibody store in 10 mM PBS, 0.5mg/ml BSA, 50% glycerol. Shipped at 4°C. Store at-20°C or -80°C. Products are valid for one natural year of receipt.Avoid repeated freeze / thaw cycles.
WB Positive detected :HEK-293 cells
Function : Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation..
Subcellular locationi :Nucleus. Chromosome, centromere.
IMPORTANT: For western blots, incubate membrane with diluted primary antibody in 1% w/v BSA, 1X TBST at 4°C overnight.