Loading...
If your product does not perform as described on this datasheet, we will refund or replace your product...
Read our guarantee »Products:Epigenetics and Nuclear Signaling >> Chromatin Remodeling >> Swi / Snf
Anti-ATRX antibody
See all ATRX products (6) ...
Mouse polyclonal to ATRX
Reacts with
Human
Fusion protein: KEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGK RKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYD SELEKEIKSMSKIGAARTTK, corresponding to amino acids 701/800 of Human ATRX.
KEVSRMSHSS SSDTDINEIH TNHKTLYDLK TQAGKDDKGK RKRKSSTSGS DFDTKKGKSA KSSIISKKKR QTQSESSNYD SELEKEIKSM SKIGAARTTK
Liquid
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze / thaw cycles.
Constituents: 50% Glycerol
Whole antiserum
This antibody was raised by a genetic immunization technique. Genetic immunization can be used to generate antibodies by directly delivering antigen-coding DNA into the animal, rather than injecting a protein or peptide (Tang et al.PubMed: 1545867; Chambers and Johnston PubMed: 12910245; Barry and Johnston PubMed: 9234514). The animal`s cells produce the protein, which stimulates the animal`s immune system to produce antibodies against that particular protein. A vector coding for a partial fusion protein was used for genetic immunisation of a mouse and the resulting serum was tested in Western blot against an E.coli lysate containing that partial fusion protein. Genetic immunization offers enormous advantages over the traditional protein-based immunization method. DNA is faster, cheaper and easier to produce and can be produced by standard techniques readily amenable to automation. Furthermore, the antibodies generated by genetic immunization are usually of superior quality with regard to specificity, affinity and recognizing the native protein.
Polyclonal
IgG
Epigenetics and Nuclear Signaling >> Chromatin Remodeling >> Swi / Snf
Western blot - ATRX antibody (ab21830)
(enlarge)
Our Abpromise guarantee covers the use of ab21830 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/1000. Predicted molecular weight: 282 kDa.
Not tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
This antibody has been tested in Western blot against an E.coli lysate containing the partial recombinant fusion protein used as an immunogen. We have no data on detection of endogenous protein.
Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.
Ubiquitous.
Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked non-deletion type (ATRX) [MIM:301040]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.
Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:309580]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.
Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:300448]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.
Belongs to the SNF2/RAD54 helicase family.
Contains 1 ADD domain.
Contains 1 GATA-type zinc finger.
Contains 1 helicase ATP-binding domain.
Contains 1 helicase C-terminal domain.
Contains 1 PHD-type zinc finger.
Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.
Phosphorylated upon DNA damage, probably by ATM or ATR.
Nucleus. Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with HP1.
Target information above from: UniProt accessionP46100
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
Western blot - ATRX antibody (ab21830)

All lanes : Anti-ATRX antibody (ab21830) at 1/1000 dilution
Lane 1 : Total protein extract from E. coli with ~50ng to 100ng of a
negative control fusion protein with an irrelevant antigen at 20 ug
Lane 2 : Total protein extract from E. coli with ~50ng to 500ng of the
antigen fusion protein at 20 ug
Secondary
Rabbit anti-mouse IgG + IgM, (H+L) horseradish peroxidase conjugated at
1/5000 dilution
Predicted band size : 282 kDa
The molecular weight of the band on the western blot does not correspond to the predicted band size above (predicted from the molecular weight of the natural protein) because of the additional mass of the fusion and because the fusion protein only contains a partial fragment of the gene.
ab21830 has not yet been referenced specifically in any publications.
Publishing research using ab21830? Please let us know so that we can cite the reference in this datasheet
Concentration of lot no. is
Concentration not available for this lot.
Find concentration of your lot:

All lanes : Anti-ATRX antibody (ab21830) at 1/1000 dilution
Lane 1 : Total protein extract from E. coli with ~50ng to 100ng of a
negative control fusion protein with an irrelevant antigen at 20 ug
Lane 2 : Total protein extract from E. coli with ~50ng to 500ng of the
antigen fusion protein at 20 ug
Secondary
Rabbit anti-mouse IgG + IgM, (H+L) horseradish peroxidase conjugated at
1/5000 dilution
Predicted band size : 282 kDa
The molecular weight of the band on the western blot does not correspond to the predicted band size above (predicted from the molecular weight of the natural protein) because of the additional mass of the fusion and because the fusion protein only contains a partial fragment of the gene.
0
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
Call 01223 696 000 or contact us
