STAT4 human
SIGMA/SRP2157 - recombinant, expressed in insect cells, ≥85% (SDS-PAGE)
Synonym: SLEB11
Product Type: Chemical
Immunoblotting STAT4 Cat. No. SRP2157: STAT4 was separated on SDS-PAGE using 1-3 μg protein (left); and a protein marker (right).
| assay | ≥85% (SDS-PAGE) |
| biological source | human |
| color | clear colorless |
| concentration | 500 μg/mL |
| form | frozen liquid |
| mol wt | ~87.7 kDa |
| NCBI accession no. | NM_003151   |
| packaging | pkg of 10 μg |
| recombinant | expressed in insect cells |
| shipped in | dry ice |
| storage condition | avoid repeated freeze/thaw cycles |
| storage temp. | −70°C |
| UniProt accession no. | Q14765 |
| Biochem/physiol Actions: | Signal transducer and activator of transcription (STAT) proteins are a family of latent cytoplasmic transcription factors involved in cytokine, hormone, and growth factor signal transduction. Seven members of the STAT family of transcription factors have been identified in mammalian cells: STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, and STAT6. STAT proteins mediate broadly diverse biologic processes, including cell growth, differentiation, apoptosis, fetal development, transformation, inflammation, and immune response. Receptor-recruited STATs are phosphorylated on a single tyrosine residue in the carboxy terminal portion. The modified STATs are released from the cytoplasmic region of the receptor subunits to form homodimers or heterodimers through reciprocal interaction between the phosphotyrosine of one STAT and the SH2 domain of another. Following dimerization, STATs rapidly translocate to the nucleus and interact with specific regulatory elements to induce target gene transcription. Recently, STAT-1 has been implicated in modulating pro- and anti-apoptotic genes following several stress-induced responses. These effects are dependent on STAT-1 phosphorylation on serine-727 and require the C-terminal transactivation domain of STAT-1 to enhance its pro-apoptotic effect or inhibit its anti-apoptotic effects. The STAT-1 C-terminal domain has been demonstrated to be important for protein-protein interaction with other transcriptional activators. The reports that STAT-1-deficient mice develop spontaneous and chemically induced tumours more rapidly compared to wild-type mice and that STAT-1-deficient cells are more resistant to agents that induce apoptosis strongly support the argument that STAT-1 acts as a tumour suppressor. |
| Physical form: | Clear and colorless frozen liquid solution |
| Preparation Note: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | ≥85% (SDS-PAGE) |
| Storage Temp. | −70°C |
| UNSPSC | 12352200 |