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SAB4200504

Sigma-Aldrich

Anti-SND1 antibody, Mouse monoclonal

clone SND1-3, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-SND1 antibody produced in mouse, Monoclonal Anti-TDRD11, Monoclonal Anti-staphylococcal nuclease and tudor domain containing 1, p100

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

SND1-3, monoclonal

form

buffered aqueous solution

mol wt

antigen ~102 kDa

species reactivity

human, rat, mouse

concentration

~1.0 mg/mL

technique(s)

western blot: 1-2 μg/mL using whole extracts of human HeLa or HEK-293T cells.

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SND1(27044)
mouse ... Snd1(56463)
rat ... Snd1(64635)

General description

Monoclonal Anti-SND1 (mouse IgG1 isotype) is derived from the hybridoma SND1-3 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide. The Staphylococcal nuclease and tudor domain containing 1 (SND1) protein is highly conserved from yeast to human. It contains five repeated staphylococcal nuclease-like domains and a tudor-like domain, probably required for its interaction with nucleic acids and proteins, respectively. The SND1 protein is a constituent of the RNA-induced silencing complex (RISC). The SND1 gene is mapped to the human chromosome location 7q31.3.

Specificity

Monoclonal Anti-SND1 recognizes human, mouse, rat, hamster and bovine SND1.

Immunogen

Synthetic peptide corresponding to an internal region of human SND1, conjugated to KLH. The corresponding sequence differs by a single amino acid in mouse and rat SND1.

Application

Monoclonal Anti-SND1 antibody produced in mouse may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence

Biochem/physiol Actions

The Staphylococcal nuclease and tudor domain containing 1 (SND1) protein is involved in the regulation of transcription. It also modulates the RNA interference (RNAi) function, RNA splicing, editing and stability. The SND1 protein promotes the degradation of hyper-edited inosine containing miRNA precursors. It modulates miRNA processing and expression through RNA editing by adenosine deaminase acting on RNA (ADAR). SND1 is up-regulated in human colon cancer, breast cancer and cancer cell lines. This protein promotes nucleic acid interaction along with protein-protein interactions. It also interacts with transcription factors as a transcriptional co-activator of Epstein-Barr virus nuclear antigen 2 (EBNA2) and signal transducer and activator of transcription (STAT5 and STAT6).

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 at -20oC in working aliquots. Repeated freezing and thawing,or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples 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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Expression analysis of Tudor-SN protein in mouse tissues
Fashe T, et al.
Tissue & cell, 45(1), 21-31 (2013)
Hasiyet Memetimin et al.
Scientific reports, 12(1), 22291-22291 (2022-12-25)
Lipoprotein lipase (LPL) hydrolyzes the triglyceride core of lipoproteins and also functions as a bridge, allowing for lipoprotein and cholesterol uptake. Transgenic mice expressing LPL in adipose tissue under the control of the adiponectin promoter (AdipoQ-LPL) have improved glucose metabolism
Role of the staphylococcal nuclease and tudor domain containing 1 in oncogenesis
Jariwala N, et al.
International Journal of Oncology, 46(2), 465-473 (2015)
Amnat Phetrungnapha et al.
Fish & shellfish immunology, 34(3), 875-884 (2013-01-22)
RNA interference (RNAi) plays a crucial role as an antiviral defense in several organisms including plants and invertebrates. An understanding of RNAi machineries especially protein components of the RNA-induced silencing complex (RISC) is essential for prior to applying RNAi as

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