M1944
Anti-MBDin/XAB1 (KP-19) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 41 kDa
species reactivity
human
technique(s)
microarray: suitable, western blot: 1:250-1:500 using nuclear extracts of HeLa cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GPN1(11321)
General description
MBD2-interacting protein (MBDin) or XPA-binding protein 1 (XAB1) GPN-loop GTPase (GPN1) comprises a conserved Gly-Pro-Asn (GPN) motif. It has an N-terminal guanosine triphosphatase (GTPase) domain or GTP binding domain, a C-terminal acidic domain and six nuclear export sequences (NES). GPN1 gene is mapped to human chromosome 2p23.3.
Immunogen
synthetic peptide corresponding to amino acids 32-50 of human XAB1, conjugated to KLH via a C-terminal added cysteine residue.
Application
Anti-MBDin/XAB1 (KP-19) antibody produced in rabbit may be used in immunoblotting.
Biochem/physiol Actions
Anti MBDin/XAB1 (KP-19) recognizes human MBDin/XAB1.
GPN-loop GTPase 1 (GPN1) interacts with RNA polymerase II assembly intermediates. The nuclear export sequence is crucial for the nuclear import of DNA-directed RNA polymerase II subunit (POLR2A and POLR2B). GPN1 mediates the nuclear localization of Xeroderma pigmentosum complementation group A (XPA). The transcriptional repression by methyl-CpG-binding domain protein 2 (MBD2) at methylated promoters are relieved by MBD2-interacting protein (MBdin).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog, 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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Humberto Reyes-Pardo et al.
Biochimica et biophysica acta, 1823(10), 1756-1766 (2012-07-17)
XAB1/Gpn1 is a GTPase that associates with RNA polymerase II (RNAPII) in a GTP-dependent manner. Although XAB1/Gpn1 is essential for nuclear accumulation of RNAPII, the underlying mechanism is not known. A XAB1/Gpn1-EYFP fluorescent protein, like endogenous XAB1/Gpn1, localized to the
Francesca Lembo et al.
Molecular and cellular biology, 23(5), 1656-1665 (2003-02-18)
We have identified a human gene encoding a novel MBD2-interacting protein (MBDin) that contains an N-terminal GTP-binding site, a putative nuclear export signal (NES), and a C-terminal acidic region. MBDin cDNA was isolated through a two-hybrid interaction screening using the
S-C Bae et al.
Zeitschrift fur Rheumatologie, 79(9), 929-936 (2020-01-23)
To investigate whether periodontitis is causally associated with risk of rheumatoid arthritis (RA) or systemic lupus erythematosus (SLE). We performed two-sample Mendelian randomization (MR) analysis using the inverse variance-weighted (IVW), weighted median, and MR-Egger regression methods on publicly available summary
Apurva R Patel et al.
Journal of controlled release : official journal of the Controlled Release Society, 213, 18-26 (2015-06-17)
3, 3-Diindolylmethane-14 (DIM-14), a novel lipophilic derivative of DIM, has demonstrated anticancer activity in different types of cancers. However, poor solubility and low oral bioavailability of DIM-14 limit its translational benefits in vivo. This study was carried out to improve
Jürgen Niesser et al.
Molecular and cellular biology, 36(5), 820-831 (2015-12-30)
Biogenesis of the 12-subunit RNA polymerase II (Pol II) transcription complex requires so-called GPN-loop GTPases, but the function of these enzymes is unknown. Here we report the first crystal structure of a eukaryotic GPN-loop GTPase, the Saccharomyces cerevisiae enzyme Npa3
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