Lane 1: Hela
Lane 2: A431
Lane 3: Mouse skeletal muscle
Lane 4: PC-12
Recombinant Rabbit monoclonal primary
Nuclear Matrix Protein p84 Recombinant Rabbit Monoclonal Antibody [JU53-18] (ET1706-52)
Synthetic peptide within human nuclear matrix protein p84 aa 367-416 / 657.
Hela, A431, mouse skeletal muscle tissue lysate, PC-12, HUVEC, LOVO, rat testis tissue, rat brain tissue, human tonsil tissue, human lung cancer tissue, human colon cancer tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Nuclear Matrix Protein p84
hTREX84 antibody; Death domain containing protein p84N5 antibody; HPR 1 antibody; HPR1 antibody; hTREX84 antibody; Nuclear matrix protein p84 antibody; P84 antibody; p84N5 antibody; Tho 1 antibody; THO complex 1 antibody; THO complex subunit 1 antibody; Tho1 antibody; THOC 1 antibody; Thoc1 antibody; THOC1_HUMAN antibody
Ubiquitous. Expressed in various cancer cell lines. Expressed at very low levels in normal breast epithelial cells and highly expressed in breast tumors. Expression is strongly associated with an aggressive phenotype of breast tumors and expression correlates with tumor size and the metastatic state of the tumor progression.
Expression is altered specifically during apoptosis and is accompanied by the appearance of novel forms with smaller apparent molecular mass.; Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.
SwissProt: Q96FV9(Human) Q8R3N6(Mouse) P59924(Rat)
THOC1 (THO complex subunit 1), also known as Tho1, P84, HPR1 or P84N5, is a 657 amino acid nuclear matrix protein and is evolutionarily conserved from yeast to humans. THOC1 contains one death domain and is a component of the heteromultimeric THO/TREX (transcription/export) complex along with THOC2, THOC3, BAT1 and ALY. The THO/TREX complex is recruited to transcribed genes and travels along with RNA polymerase II (Pol II) during elongation, coupling elongating Pol II with RNA splicing and export factors. THOC1 is expressed at high levels in breast cancer cells and at relatively low levels in normal epithelia. A reduction of THOC1 in cancer cell lines results in reduced cell proliferation. This suggests that cancer cells are dependent on the high levels of THOC1 expression and therefore THOC1 may be a good target for cancer therapy.