AFfirm™ SND1 Mouse Monoclonal Antibody - #BF8569

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Product: SND1 Mouse Monoclonal Antibody
Catalog: BF8569
Description: Mouse monoclonal antibody to SND1
Application: WB
Reactivity: Human, Rat
Mol.Wt.: 100~120kD; 102kD(Calculated).
Uniprot: Q7KZF4

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 100ul $280 In stock
 200ul $350 In stock

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Related Downloads
MS Report
HPLC Report
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Mouse
Application:
WB 1:500-1:3000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Rat
Clonality:
Monoclonal [AFfirm8569]
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

100 kDa coactivator; EBNA 2 co activator (100kD); EBNA2 coactivator p100; p100; p100 co-activator; p100 coactivator; p100 EBNA2 co activator; SND 1; Snd1; SND1_HUMAN; Staphylococcal nuclease and tudor domain containing 1; Staphylococcal nuclease domain containing 1; Staphylococcal nuclease domain containing protein 1; Staphylococcal nuclease domain-containing protein 1; TDRD11; TRD 11; TRD11; Tudor domain containing protein 11; Tudor domain-containing protein 11;

Immunogens

Immunogen:

A synthesized peptide derived from Human SND1.

Uniprot:

Q7KZF4(SND1_HUMAN) >>Visit HPA database.

Gene(ID):
SND1(27044)
Expression:
Q7KZF4 SND1_HUMAN:

Ubiquitously expressed.

Sequence:
MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR

Research Backgrounds

Function:

Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs. As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition. Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for STAT5 (By similarity).

(Microbial infection) Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).

PTMs:

Phosphorylated by PIM1 in vitro.

Subcellular Location:

Cytoplasm. Nucleus. Melanosome.
Note: In IL-4 stimulated cells colocalizes with STAT6 in the nucleus (PubMed:12234934). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitously expressed.

Subunit Structure:

Forms a ternary complex with STAT6 and POLR2A. Associates with the RNA-induced silencing complex (RISC). Interacts with the RISC components AGO2, FMR1 and TNRC6A. Interacts with GTF2E1 and GTF2E2. Interacts with PIM1. Interacts with STAT5 (By similarity). Interacts with SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By similarity).

(Microbial infection) Interacts with EAV NSP1. Binds to acidic transactivation domain of EBNA2.

Research Fields

· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

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