SSR2/TRAP Beta Polyclonal

Membrane receptor signaling by various ligands, including interferons and growth hormones such as EGF, induces activation of JAK kinases which then leads to tyrosine phosphorylation of proteins that have been designated Stats (signal transducers and activators of transcription. The first members of this family to be described include Stat1α p91, Stat1β p84 (a form of p91 that lacks 38 COOH-terminal amino acids) and Stat2 p113. Stat1 and Stat2 are induced by IFN-α and form a heterodimer which is part of the ISGF3 transcription factor complex. Stat3, which becomes activated in response to epidermal growth factor (EGF) and interleukin-6 (IL-6), but not interferon-γ (IFN-γ) or Stat4, is an The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum (ER) membrane receptor associated with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum (ER) membrane receptor associated with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23.