|Detection of Human GRAIL/RNF128 by Western Blot. Western blot shows lysates of MCF‑7 human breast cancer cell line. PVDF Membrane was probed with 1 µg/mL of Human GRAIL/RNF128 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6234) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for GRAIL/RNF128 at approximately 45 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
GRAIL (Gene related to anergy in lymphocytes protein; also RNF128) is a 45-47 kDa, type I transmembrane E3 ubiquitin ligase. It is expressed in the endosomes of select cell types such as early myeloid progenitors and lymphocytes, and mediates the ubiquitination of membrane proteins such as CD3, CD40L, and CD83, plus the tetraspanins CD81 and CD151. GRAIL apparently regulates the threshold for T cell activation, and as such, plays a key role in autoimmunity. In Treg cells, GRAIL promotes suppressive activity by restricting Th17 gene expression. Mature human GRAIL is 390 amino acids (aa) in length (aa 39-428). It possesses a 169 aa luminal region (aa 39-207) and a 190 aa cytoplasmic domain. The luminal region contains one PA (protease-associated) domain that mediates protein-protein interactions (aa 48-193), and the cytoplasmic segment shows one zinc-finger region (aa 277-318). There is one splice variant that shows a 134 aa substitution for aa 1-161. Over aa 42-161, human GRAIL shares 98% aa identity with mouse GRAIL.
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