SSSCA1 Human
Description
Product Specs
Product Science Overview
Sjögren Syndrome/Scleroderma Autoantigen 1 (SSSCA1) is a protein that has garnered significant interest in the medical and scientific communities due to its association with autoimmune diseases such as Sjögren’s syndrome and scleroderma. This article delves into the background, molecular structure, and significance of SSSCA1, particularly in the context of human recombinant technology.
SSSCA1 was first identified in the late 1990s as a novel autoantigen overexpressed in patients with Sjögren’s syndrome and scleroderma . The human SSSCA1 gene is located on chromosome 11 (11q13.1) and encodes a small soluble protein of approximately 21.5 kDa . The protein features a predicted N-terminal zinc ribbon domain type 2 (ZNRD2) and an unknown domain in the C-terminus .
Recent studies have provided a detailed characterization of SSSCA1 at the molecular, structural, and subcellular levels . The crystal structure of the zinc ribbon domain type 2 (ZNRD2) has been determined at a resolution of 2.3 Å . The C-terminal domain of SSSCA1 serves a dual function: it acts as an interaction site for Tankyrase 1 (TNKS1) and also functions as a nuclear export signal . TNKS1 is identified as a direct binding partner of SSSCA1, with the binding site mapped to the ankyrin repeat cluster 2 (ARC2) of TNKS1 .
SSSCA1 has been linked to mitosis and centromere association, making it a potential marker candidate in diverse solid cancers . Its overexpression in Sjögren’s syndrome and scleroderma patients suggests a role in the pathogenesis of these autoimmune diseases . Sjögren’s syndrome is characterized by the presence of autoantibodies targeting a wide array of organ and non-organ specific autoantigens, with SSSCA1 being one of the notable targets .
Human recombinant technology involves the use of recombinant DNA techniques to produce human proteins in various expression systems, such as Escherichia coli. SSSCA1 has been successfully expressed in E. coli, allowing for detailed structural and functional studies . This technology facilitates the production of large quantities of the protein, which is essential for research and potential therapeutic applications.
