SSR4 Antibodies

Structure of SSR4

SSR4 is a membrane protein with a molecular weight of approximately 20 kDa, and its precise molecular weight varies by species. This protein is a key subunit of the signal recognition granule receptor (SRP receptor) and is mainly located on the endoplasmic reticulum membrane.

The SSR4 protein contains approximately 180 amino acids and has a transmembrane helical structure and a cytoplasmic domain. Its core function is to form a complex with the SSR1 and SSR3 subunits, and mediate the directional transport of the nascent peptide chain to the endoplasmic reticulum by recognizing the signal sequence in the signal recognition particle (SRP). The N-terminal domain of the protein is responsible for interacting with ribosomes, while the C-terminal domain is involved in the receptor dimerization process. Mutations in this protein can lead to congenital glycosylation disorders, affecting the normal synthesis and secretion of various proteins.

Fig. 1 Schematic diagram of the SSR4 secondary structure.¹

Key structural properties of SSR4:

• Single transmembrane helical domain
• Conserved cytoplasmic side C-terminal domain
• Endoplasmic reticulum localization signal peptide sequence

Functions of SSR4

The main function of the protein encoded by the SSR4 gene is to participate in the protein targeted transport process related to the endoplasmic reticulum. In addition, it also involves a variety of cell biological processes, including protein quality control and the regulation of cell secretion pathways.

SSR4 forms heterologous complexes with other subunits such as SSR1 and SSR3, interacting with signal recognition particles (SRP) and ribosomes in a GTP-dependent manner, demonstrating highly temporal and spatial regulatory characteristics. Its dysfunction is closely related to a variety of hereditary metabolic diseases.

Applications of SSR4 and SSR4 Antibody in Literature

1. Zhang, Jiaqi, et al. "Unveiling SSR4: a promising biomarker in esophageal squamous cell carcinoma." Frontiers in Immunology 16 (2025): 1544154. https://doi.org/10.3389/fimmu.2025.1544154

The article indicates that SSR4 is highly expressed in esophageal squamous cell carcinoma and is associated with lymph node metastasis and poor prognosis. It affects the infiltration of immune cells in the tumor microenvironment, especially plasma cells, by regulating the MIF/CD74/CXCR4 axis, and is expected to become a potential target for the diagnosis and treatment of ESCC.

2. Sun, Wenqiang, X Zhu. "A novel SSR4 variant associated with congenital disorder of glycosylation: a case report and related analysis." Frontiers in Genetics 15 (2024): 1402883. https://doi.org/10.3389/fgene.2024.1402883

Research has found that the c.80_96del deletion mutation of the SSR4 gene leads to congenital disorder of glycosylation (CDG), and patients present with multiple system symptoms such as growth retardation. Down-regulation of SSR4 expression affects pathways such as coagulation, red blood cell development and muscle regulation. High-calorie nutritional support can improve prognosis.

3. Wang, Jun, et al. "Case Report: The novel hemizygous mutation in the SSR4 gene caused congenital disorder of glycosylation type iy: A case study and literature review." Frontiers in Genetics 13 (2022): 955732. https://doi.org/10.3389/fgene.2022.955732

This study reports for the first time that the novel variant c.269G>A of the SSR4 gene in the Chinese population causes congenital glycosylation disorder. The patient presented with typical symptoms such as intellectual and motor retardation and microcephaly, and the expression of SSR4 decreased significantly. This discovery expands the mutation and clinical spectrum of SSR4-CDG.

4. Lien, Joan Chern-Hui, et al. "Hemizygous Contiguous Gene Deletion within Xq28 that includes BCAP31, ABCD1, SRPK3 and SSR4: Case Report and Literature Review." Global Medical Genetics (2025): 100066. https://doi.org/10.1016/j.gmg.2025.100066

Research has found that a 110kb deletion in the Xq28 chromosomal region (including genes such as SSR4) can lead to severe neonatal syndrome, presenting with new phenotypes such as cleft lip and palate and vascular rings. The co-deletion of SSR4 and adjacent genes is the main cause of the disease. This study has deepened the understanding of Xq28 deletion syndrome.

5. Li, Haixia, Jianjun Wang, and Juchuanli Tu. "A-to-I nonsynonymous RNA editing was significantly enriched in the ubiquitination site and correlated with clinical features and immune response." Scientific Reports 12.1 (2022): 15079. https://doi.org/10.1038/s41598-022-18926-x

Studies have found that RNA asynchronous editing (A-TO-I) is significantly enriched in ubiquitination sites. Among them, the editing levels of genes such as SSR4 vary significantly in tumors and are related to clinical prognosis and immune response pathways, providing A new target for cancer diagnosis and treatment.

Creative Biolabs: SSR4 Antibodies for Research

Creative Biolabs specializes in the production of high-quality SSR4 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom SSR4 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our SSR4 antibodies, custom preparations, or technical support, contact us at email.