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SET Domain Containing 8 Pseudogene 1 (SETD8P1) (C-Term), (AA 289-317) antibody

Details for Product No. ABIN387998
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Antigen
Epitope
C-Term, AA 289-317
(1)
Reactivity
Human
(1), (1)
Host
Rabbit
(1)
Clonality (Clone)
Polyclonal ()
Application
Western Blotting (WB)
(1), (1)
Pubmed 5 references available
Quantity 400 µL
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Catalog No. ABIN387998
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Immunogen This SET7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 289-317 AA from the C-terminal region of human SET7.
Clone RB5744
Isotype Ig
Specificity This SET7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 296~326 amino acids from the C-terminal region of human SET7.
Purification This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Alternative Name SET7
Background Histone methyltransferases (HMTases) selectively methylate evolutionarily conserved arginine or lysine residues, primarily in the N-terminal tails of histones H3 and H4. Signal transduction pathways affecting the N-terminal tails of histones lead to a number of post-translational modifications including acetylation, phosphorylation, poly(ADP-ribosylation), ubiquitination and methylation. These modifications play critical roles in regulating chromatin structure and gene expression. Set7/9 is a histone specific HMTase that methylates histone H3 lysine 4. Set7/9 transfers methyl groups to lysine 4 of histone H3 in complex with S-adenosyl-L-methionine. In yeast, H4-K20 methylation does not have any apparent role in the regulation of gene expression or heterochromatin function, rather it appears to play a role in DNA damage response. Loss of Set9 activity or mutation of H4-K20 markedly impairs yeast cell survival after genotoxic challenge and compromises the ability of cells to maintain checkpoint mediated cell cycle arrest. Genetic experiments link Set9 to Crb2, a homolog of the mammalian checkpoint protein 53BP1, and the enzyme is required for Crb2 localization to sites of DNA damage.
Synonyms: Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, KMT7
Molecular Weight 40721 DA
Gene ID 80854
UniProt Q8WTS6
Research Area Signaling, Protein Modifications, Cell Cycle, Transcription Factors, Chromatin, Cell Structure
Application Notes WB = 1:1000
Restrictions For Research Use only
Format Liquid
Concentration 2 mg/mL
Buffer PBS with 0.09 % (W/V) sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Expiry Date 6 months
Supplier Images
anti-SET Domain Containing 8 Pseudogene 1 (SETD8P1) (C-Term), (AA 289-317) antibody Western blot analysis of anti-SET7 Pab(ABIN387998) in mouse brain tissue lysate (35 µg/lane). SET7(arrow) was detected using the purified polyclonal antibody (1:70 dilution).
Background publications Nishioka, Chuikov, Sarma et al.: "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation." in: Genes & development, Vol. 16, Issue 4, pp. 479-89, 2002 (PubMed).

Kwon, Chang, Kwak et al.: "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet." in: The EMBO journal, Vol. 22, Issue 2, pp. 292-303, 2003 (PubMed).

Xiao, Jing, Wilson et al.: "Structure and catalytic mechanism of the human histone methyltransferase SET7/9." in: Nature, Vol. 421, Issue 6923, pp. 652-6, 2003 (PubMed).

Wysocka, Myers, Laherty et al.: "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." in: Genes & development, Vol. 17, Issue 7, pp. 896-911, 2003 (PubMed).

Chuikov, Kurash, Wilson et al.: "Regulation of p53 activity through lysine methylation." in: Nature, Vol. 432, Issue 7015, pp. 353-60, 2004 (PubMed).

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