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S4445

Sigma-Aldrich

Anti-Sin3A, N-terminal antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 160 kDa

species reactivity

human, rat, mouse

technique(s)

immunoprecipitation (IP): 5-10 μL using HEK 293T cell lysates
indirect immunofluorescence: 1:50-1:100 using A549cells fixed with paraformaldehyde-Triton
microarray: suitable
western blot: 1:500-1:1,000 using HeLa nuclear extracts

UniProt accession no.

compatibility

for use with ABI 7900 Fast

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SIN3A(25942)
mouse ... Sin3a(20466)
rat ... Sin3a(363067)

General description

SIN3 transcription regulator family member A (Sin3A) codes for an isoform of the transcription regulator, sin3. This 1273 amino acid protein contains a paired amphipathic helix (PAH) domain. Sin3A is located on human chromosome 15q24.

Specificity

Anti-Sin3A, N-terminal specifically recognizes mammalian Sin3A (160 kDa).

Immunogen

synthetic peptide corresponding to amino acids 1-18 of human Sin3A, conjugated to KLH via a C-terminal added cysteine residue. The immunizing peptide is conserved in human, mouse, and rat. It is not present in Sin3B.

Application

Anti-Sin3A, N-terminal antibody produced in rabbit may be used in:
  • immunoblotting
  • immunofluorescence
  • immunoprecipitation
  • chromatin immunoprecipitation (ChIP)[1]

Biochem/physiol Actions

SIN3 transcription regulator family member A (Sin3A) is identified in mouse as protein required for the transcription and growth suppressor functions of the mitotic arrest deficient protein 1 (Mad1) and MX dynamin-like GTPase 1 (Mx1) proteins. Several transcription repressors exert their effects by recruitment of the Sin3A/ histone deacetylase (HDAC) complex. Repression of transcription by the Sin3A/HDAC complex can yet be achieved through its interaction with O-GlcNAc transferase (OGT), Sin3A targets OGT to promoters, inactivating transcription factors and RNA polymerase II through the addition of O-GlcNAc residues. The paired amphipathic helix (PAH) domains of Sin3A is very much essential for protein-protein interactions. This epigenetic regulator mediates in connecting methionine metabolism and histone modification. SIN3A mutation is associated with Witteveen-Kolk syndrome.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilu-tions should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Novel SIN3A mutation identified in a Japanese patient with Witteveen-Kolk syndrome
Narumi KY, et al.
European Journal of Medical Genetics, 62(9), 103547-103547 (2019)
Same agent, different messages: insight into transcriptional regulation by SIN3 isoforms
Chaubal A and Pile LA
Epigenetics & Chromatin, 17-17 (2018)
Winfred Stacey et al.
PloS one, 11(9), e0161430-e0161430 (2016-09-03)
E2 attenuates inflammatory responses by suppressing expression of pro-inflammatory genes. Given that inflammation is increasingly being associated with neurodegenerative and psychiatric processes, we sought to elucidate mechanisms by which E2 down-regulates a component of an inflammatory response, cyclooxygenase- 2 (COX-2)

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