TDRD1 Antibody [FITC]

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-11488

Novus Biologicals, part of Bio-Techne
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NBP2-11488
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Key Product Details

Species Reactivity

Human, Mouse, Rat

Applications

ELISA, Immunohistochemistry, Immunoprecipitation, Western Blot

Label

FITC (Excitation = 495 nm, Emission = 519 nm)

Antibody Source

Polyclonal Rabbit IgG

Concentration

0.5 mg/ml

View all TDRD1 Antibodies »

Product Specifications

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

Clonality

Polyclonal

Host

Rabbit

Isotype

IgG

Applications for TDRD1 Antibody [FITC]

Application
Recommended Usage

ELISA

1:500

Western Blot

1:10000

Formulation, Preparation, and Storage

Purification

Immunogen affinity purified

Formulation

Tris/Glycine buffer, pH 7.4-7.8, HEPES,BSA 0.5%, glycerol 30%.

Preservative

0.02% Sodium Azide

Concentration

0.5 mg/ml

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

Background: TDRD1

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).

Long Name

Tudor Domain Containing 1

Alternate Names

CT41.1

Gene Symbol

TDRD1

Additional TDRD1 Products

Product Documents for TDRD1 Antibody [FITC]

Product Datasheets

Certificate of Analysis

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Product Specific Notices for TDRD1 Antibody [FITC]

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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