Myeloid/lymphoid Or Mixed-Lineage Leukemia (Trithorax Homolog, Drosophila); Translocated To, 4 (MLLT4) (AA 1091-1233) antibody

Antigen: Myeloid/lymphoid Or Mixed-Lineage Leukemia (Trithorax Homolog, Drosophila); Translocated To, 4 (MLLT4)

Synonyms: AF6, AF-6, AFADIN, FLJ34371, RP3-431P23.3, Gm314, Afadin, I-afadin, S-afadin, 5033403D15Rik, Af6, MLLT4, mllt4

Binding Site: AA 1091-1233

Clonality: Monoclonal (35)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF)

Catalog no.: ABIN968144

Additional Information

Alternative name: AF6

Immunogen: Human AF6

Cross-Reactivity: Rat (Rattus), Mouse (Murine)

Format: Liquid

Isotype: IgG2a

Clone: 35

Description: AF6 (ALL-1 Fusion partner in chromosome 6) was discovered as the fusion partner of ALL-1. These genes undergo translocation and fusion in acute myeloid leukemias. AF6, or p180, was also identified as a Ras-interacting protein isolated from bovine brain. AF6 binds to the GTP-Ras but not to the inactive GDP, or ineffective forms of Ras. The interaction between AF6 and Ras may regulate the Ras signaling pathway since this association was prevented by the binding of c-Raf-1 to Ras. The Ras-binding site is located within amino acids 36-206 of AF6. AF6 is 1612 amino acids in length with homology to the DLG family of proteins located in cell-cell junctions, suggesting AF6 might be important in cell-to-cell communicative events. Furthermore, AF6 has the GLGF motif characteristic of DLG proteins that include Drosophilia's Canoe, implicated in the developmental pathway triggered by Notch activation. Like AF6, Canoe was also identified as a Ras-binding protein. The amino acid sequence and biochemical property similarities between Canoe and AF6 indicate that the latter may be important in developmental processes regulated by Ras.
Synonyms: ALL-1 Fusion partner in chromosome 6

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Please refer to us for technical protocols.

Molecular Weight: 182 kDa

Comments:

Related Products: ABIN968545, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20°C.

Restrictions: For Research Use only

Images

Western blot analysis of AF6 on a PC-12 cell lysate (Rat neuroblastoma, ATCC CRL-1721). Lane 1: 1:125, lane 2: 1:250, lane 3: 1:500 dilution of the mouse anti-AF6 antibody.

Immunofluorescence staining of mouse macrophages.

Publications

Product: Prasad, Gu, Alder et al.: "Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation." in: Cancer research, Vol. 53, Issue 23, pp. 5624-8, 1994 (PubMed).

Kuriyama, Harada, Kuroda et al.: "Identification of AF-6 and canoe as putative targets for Ras." in: The Journal of biological chemistry, Vol. 271, Issue 2, pp. 607-10, 1996 (PubMed).

Buchert, Schneider, Meskenaite et al.: "The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain." in: The Journal of cell biology, Vol. 144, Issue 2, pp. 361-71, 1999 (PubMed).

Cordenonsi, DAtri, Hammar et al.: "Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3, and myosin." in: The Journal of cell biology, Vol. 147, Issue 7, pp. 1569-82, 2000 (PubMed).

Ebnet, Schulz, Meyer Zu Brickwedde et al.: "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1." in: The Journal of biological chemistry, Vol. 275, Issue 36, pp. 27979-88, 2000 (PubMed).