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RUNX1 antibody (Runt-Related Transcription Factor 1) (AA 200-260)

Details for Product anti-RUNX1 Antibody No. ABIN350816, Supplier: Log in to see
Antigen
  • AI462102
  • aml
  • aml-1
  • aml1
  • Aml1
  • AML1
  • AML1-EVI-1
  • aml1-evi-1
  • AMLCR1
  • amlcr1
  • cbfa2
  • Cbfa2
  • CBFA2
  • EVI-1
  • evi-1
  • Pebp2a2
  • PEBP2aB
  • pebp2ab
  • Pebpa2b
  • Runx-1
  • runx1
  • RUNX1
  • runxa
  • XAML
  • Xaml1
Epitope
AA 200-260
20
16
15
14
13
11
10
10
10
10
9
9
6
6
5
5
4
3
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human, Rat (Rattus), Mouse (Murine)
251
97
81
8
8
7
5
4
3
3
2
2
1
1
Host
Rabbit
188
64
3
2
1
Clonality
Polyclonal
Conjugate
This RUNX1 antibody is un-conjugated
6
5
5
3
3
3
3
3
3
3
3
3
3
2
2
Application
Immunohistochemistry (IHC), Western Blotting (WB)
202
127
70
58
44
33
21
18
7
6
3
3
1
1
1
Supplier
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Immunogen A synthetic peptide from aa region 200-260 of human Runx1 conjugated to an immunogenic carrier protein was used as the antigen. The peptide is homologous in rat and mouse.
Specificity Specific for Runx1.
Purification Whole serum
Alternative Name Runx1 (RUNX1 Antibody Abstract)
Background Function: CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and GM-CSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. Isoform AML-1L interferes with the transactivation activity of RUNX1. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the mouse BLK promoter. Inhibits MYST4-dependent transcriptional activation.
Subunit: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Isoform AML-1L can neither bind DNA nor heterodimerize. Interacts with TLE1 and THOC4. Interacts with ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with MYST3 and MYST4. Interacts with SUV39H1, leading to abrogate the transactivating and DNA-binding properties of RUNX1.
Tissue specificity: Highest levels in thymus, bone marrow and peripheral blood. Also known as: Runx1, Core-binding factor, alpha 2 subunit, CBF-alpha 2, Acute myeloid leukemia 1 protein, Oncogene AML-1, Polyomavirus enhancer-binding protein 2 alpha B subunit, PEBP2-alpha B, PEA2-alpha B, SL3-3 enhancer factor 1 alpha B subunit, SL3/AKV core-binding factor alpha B subunit, AML1, CBFA2.
Application Notes A dilution of 1 : 300 to 1 : 2000 is recommended.
The optimal dilution should be determined by the end user.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Supplier Images
 image for anti-RUNX1 antibody (Runt-Related Transcription Factor 1) (AA 200-260) (ABIN350816) IF on mouse cerebellum (4% PFA fixed, frozen section) at 1 : 500 dilution using Rabbi...
 image for anti-RUNX1 antibody (Runt-Related Transcription Factor 1) (AA 200-260) (ABIN350816) IF on mouse cerebellum (4% PFA fixed, frozen section) at 1 : 500 dilution using Rabbi...
 image for anti-RUNX1 antibody (Runt-Related Transcription Factor 1) (AA 200-260) (ABIN350816) IF on rat DRG (postnatal day 7) at 1 : 500 dilution using Rabbit antibody to human, r...
Background publications Baeckstroem, Wolf-Watz, Grundstroem, Haerd, Grundstroem, Sauer: "The RUNX1 Runt domain at 1.25A resolution: a structural switch and specifically bound chloride ions modulate DNA binding." in: Journal of molecular biology, Vol. 322, Issue 2, pp. 259-72, 2002

Tahirov, Inoue-Bungo, Morii, Fujikawa, Sasaki, Kimura, Shiina, Sato, Kumasaka, Yamamoto, Ishii, Ogata: "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta." in: Cell, Vol. 104, Issue 5, pp. 755-67, 2001

Zhang, Bae, Huang, Fu, Lu, Ahn, Kanno, Kanno, Ito: "A novel transcript encoding an N-terminally truncated AML1/PEBP2 alphaB protein interferes with transactivation and blocks granulocytic differentiation of 32Dcl3 myeloid cells." in: Molecular and cellular biology, Vol. 17, Issue 7, pp. 4133-45, 1997

Ghozi, Bernstein, Negreanu, Levanon, Groner: "Expression of the human acute myeloid leukemia gene AML1 is regulated by two promoter regions." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, Issue 5, pp. 1935-40, 1996

Levanon, Negreanu, Bernstein, Bar-Am, Avivi, Groner: "AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization." in: Genomics, Vol. 23, Issue 2, pp. 425-32, 1995

Zhu, Yeadon, Burden: "AML1 is expressed in skeletal muscle and is regulated by innervation." in: Molecular and cellular biology, Vol. 14, Issue 12, pp. 8051-7, 1994

Bae, Yamaguchi-Iwai, Ogawa, Maruyama, Inuzuka, Kagoshima, Shigesada, Satake, Ito: "Isolation of PEBP2 alpha B cDNA representing the mouse homolog of human acute myeloid leukemia gene, AML1." in: Oncogene, Vol. 8, Issue 3, pp. 809-14, 1993

Nucifora, Birn, Espinosa, Erickson, LeBeau, Roulston, McKeithan, Drabkin, Rowley: "Involvement of the AML1 gene in the t(3,21) in therapy-related leukemia and in chronic myeloid leukemia in blast crisis." in: Blood, Vol. 81, Issue 10, pp. 2728-34, 1993

Daga, Tighe, Calabi: "Leukaemia/Drosophila homology." in: Nature, Vol. 356, Issue 6369, pp. 484, 1992

Miyoshi, Shimizu, Kozu, Maseki, Kaneko, Ohki: "t(8,21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 23, pp. 10431-4, 1992