TDRD1 Antibody [FITC] Summary
| Immunogen |
Synthetic peptide taken within amino acid region 570-605 on TDRD1 protein. |
| Epitope |
aelleycnapksrppyrprigdac |
| Specificity |
This antibody detects multiple bands of approximate MW of 83, 94, and a minor 114kDa in TDRD1 samples. The antibody does not cross reacts with other histones or DNA binding proteins |
| Isotype |
IgG |
| Clonality |
Polyclonal |
| Host |
Rabbit |
| Gene |
TDRD1 |
| Purity |
Immunogen affinity purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
| Dilutions |
- ELISA 1:500
- Immunohistochemistry
- Immunoprecipitation
- Western Blot 1:10000
|
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
Tris/Glycine buffer, pH 7.4-7.8, HEPES,BSA 0.5%, glycerol 30%. |
| Preservative |
0.02% Sodium Azide |
| Concentration |
0.5 mg/ml |
| Purity |
Immunogen affinity purified |
Alternate Names for TDRD1 Antibody [FITC]
Background
Tudor domains are protein modules that mediate protein-protein interactions, potentially by binding to methylated ligands. There are 9 Tudor domain containing proteins (TDRD1-TDRD9) each forming hetero-complexes for epigenetic regulations in gene expression. Tudor domains are found in many eukaryotic organisms and have been implicated in protein-protein interactions in which methylated protein substrates bind to these domains. For example, the Tudor domain of Survival of Motor Neuron (SMN) binds to symmetrically dimethylated arginines of arginine-glycine (RG) rich sequences found in the C-terminal tails of Sm proteins. The SMN protein is linked to spinal muscular atrophy. Another example is the tandem tudor domains of 53BP1, which bind to histone H4 specifically dimethylated at Lys20 (H4-K20me2). Cell signaling pathways rely heavily on modular proteins containing protein-protein interaction domains to sense, transmit and process signals that regulate cellular functions. Arginine methylation modulates diverse cellular processes and represents a molecular signature of germ-line-specific Piwi family proteins. A subset of Tudor domains recognize arginine methylation modifications. Three types of arginine methylation-namely, monomethylation, asymmetrical dimethylation, and symmetrical dimethylation-are catalyzed by type I or type II protein arginine methyltransferases (PRMTs). Among these, PRMT5 is considered the major PRMT that induces symmetrical dimethylation of arginine residues on target proteins (1). The Tudor domain-containing proteins poss es RNA binding capacity which suggest they pay a role in RNA metabolism. The first well characterized Tudor-KH containing protein was studied in Fragile X mental retardation protein (FMRP), the Tudor KH domain containing proteins acts as specific scaffolding proteins involved in methylation signal and RNA processing (2). The Tdrd gene family constitutes an essential class of spermatogenesis genes with each member having a distinct function at different differentiation stages. TDRD1 gene is expressed in different splice variants by use of alternate initiation sites. The TDRD1 proteins regulate the piwi-interacting RNA (piRNA) pathways to establish retrotransposon silencing in fetal prospermatogonia (3).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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