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AB137622

Anti-SMYD5 antibody - C-terminal

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(2 Publications)

Rabbit Polyclonal SMYD5 antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human SMYD5 aa 300 to C-terminus.

View Alternative Names

RAI15, SMYD5, Protein-lysine N-trimethyltransferase SMYD5, Protein NN8-4AG, Retinoic acid-induced protein 15, SET and MYND domain-containing protein 5, [histone H3]-lysine20 N-trimethyltransferase SMYD5, [histone H4]-lysine36 N-trimethyltransferase SMYD5

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SMYD5 antibody - C-terminal (AB137622)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SMYD5 antibody - C-terminal (AB137622)

ab137622 at a 1/100 dilution, staining SMYD5 in paraffin embedded NCI-N87 xenograft tissue by Immunohistochemistry.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human SMYD5 aa 300 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q6GMV2

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

SMYD5 also known as SET and MYND domain-containing protein 5 functions as a histone methyltransferase and plays a role in regulating gene expression. It typically adds methyl groups to lysine residues on histone proteins which influences chromatin structure and gene transcription. SMYD5 has a mass of around 58 kDa and is found in various tissues with significant expression in the heart skeletal muscle and testis. Its specific localization to these tissues highlights its potential importance in the regulation of gene expression patterns that are tissue-specific.
Biological function summary

SMYD5 engages in modifying chromatin architecture which impacts cellular processes like proliferation and differentiation. It forms part of larger complexes that work in coordination to modify histones including the modification of H4K20 an important target of SMYD5's methyltransferase activity. This modification is linked to the regulation of DNA damage response and cell cycle progression. As a component of these complexes SMYD5 interacts with other proteins to execute its function.

Pathways

Research identifies SMYD5 as an important regulator in the NF-κB signaling pathway a pathway pivotal for immune response and inflammation. By influencing this pathway SMYD5 affects cellular reactions to stress and immune signals. It is known to interact with TAK1 a kinase involved in activating NF-κB demonstrating a connection with inflammatory regulation. Additionally SMYD5 has roles in the epigenetic landscape participating in pathways involving SET domain proteins responsible for chromatin remodeling.

SMYD5 has been linked to inflammatory and cancer-related conditions. The regulation of the NF-κB pathway by SMYD5 implicates it in inflammation-related diseases including rheumatoid arthritis where NF-κB activity correlates with inflammatory responses. Furthermore alterations in SMYD5 expression or function might influence tumorigenesis. In these contexts proteins like TAK1 become important as they connect SMYD5 function to key pathways driving disease development. Understanding SMYD5's role offers potential avenues for therapeutic intervention in related conditions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Protein-lysine N-trimethyltransferase that specifically catalyzes trimethylation of 'Lys-22' of the RPL40/eL40 subunit of the 60S ribosome, thereby promoting translation elongation and protein synthesis (PubMed : 39048817, PubMed : 39103523). May also act as a histone methyltransferase in the context of histone octamers, but not on nucleosome substrates : trimethylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 to form H3K36me3 and H4K20me3, respectively (By similarity). The histone methyltransferase activity, which is independent of its SET domain, is however unsure in vivo (PubMed : 39048817, PubMed : 39103523). In association with the NCoR corepressor complex, involved in the repression of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages, possibly by catalyzing the formation of H4K20me3 at the gene promoters (By similarity). Plays an important role in embryonic stem (ES) cell self-renewal and differentiation (By similarity). Maintains genome stability of ES cells during differentiation through regulation of heterochromatin formation and repression of endogenous repetitive DNA elements by promoting H4K20me3 marks (PubMed : 28951459). Acts as a regulator of the hypothermia response : its degradation in response to mild hypothermia relieves the formation of H3K36me3 at gene promoters, allowing expression of the neuroprotective gene SP1 (By similarity).
See full target information SMYD5

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 42:112234 PubMed36897778

2023

The lysine methyltransferase SMYD5 amplifies HIV-1 transcription and is post-transcriptionally upregulated by Tat and USP11.

Applications

Unspecified application

Species

Unspecified reactive species

Daniela Boehm,Victor Lam,Martina Schnolzer,Melanie Ott

Biochimica et biophysica acta 1854:1816-1822 PubMed26410624

2015

Master redox regulator Trx1 upregulates SMYD1 & modulates lysine methylation.

Applications

WB

Species

Human

Tong Liu,Changgong Wu,Mohit Raja Jain,Narayani Nagarajan,Lin Yan,Huacheng Dai,Chuanlong Cui,Ahmet Baykal,Stacey Pan,Tetsuro Ago,Junichi Sadoshima,Hong Li
View all publications

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