Monoclonal Antibodies

The SDCBP monoclonal antibody is produced through a meticulous process. Mice are immunized with recombinant human SDCBP protein (amino acids 2-298), and B cells are isolated from their spleens. These B cells are then fused with myeloma cells to create hybridomas. Through careful screening, the hybridoma cell line that produces the SDCBP antibody is selected and cultured in the mouse abdominal cavity. The purified SDCBP monoclonal antibody is subsequently obtained from the mouse ascites using protein G affinity chromatography, guaranteeing a purity exceeding 95%. This unconjugated IgG2b antibody exhibits reactivity across three species: human, mouse, and rat, making it suitable for applications such as ELISA and Western blotting.

SDCBP, also recognized as Syntenin-1, is a multifaceted protein involved in a diverse array of cellular processes, including cell adhesion, migration, and signaling. Acting as a scaffolding protein, SDCBP interacts with a range of membrane and cytoplasmic proteins, such as syndecans, integrins, and signaling molecules, to form multi-protein complexes. These complexes play a crucial role in the regulation of cell-cell and cell-matrix interactions, as well as in modulating intracellular signaling pathways, including those governed by the Wnt and TGF-β signaling pathways. SDCBP has also been implicated in the regulation of endocytosis, exocytosis, and vesicular trafficking.

The MCM9 monoclonal antibody is generated through a process that begins with the immunization of mice using recombinant human MCM9 protein (amino acids 1-391). The resulting hybridoma cells, produced by fusing immunized mouse B cells with myeloma cells, secrete the specific MCM9 antibody. After isolation from mouse ascites, the MCM9 monoclonal antibody undergoes purification using protein G affinity chromatography, achieving a high purity level of 95%⁺. This unconjugated IgG1 antibody is well-suited for detecting the presence of human MCM9 protein in various applications, including ELISA, Western blotting (WB), and immunohistochemistry (IHC).

MCM9 functions as a crucial component of the MCM complex, playing a vital role in homologous recombination repair of double-strand DNA breaks. Its involvement is essential for the proper formation of meiotic recombination intermediates, which are critical for accurate chromosome segregation during meiosis. MCM9 also contributes to maintaining genomic stability by preventing the accumulation of DNA damage. Mutations in the MCM9 gene have been linked to a rare genetic disorder known as primary ovarian insufficiency (POI).

This monoclonal antibody is produced using a recombinant human SLN protein (1-31aa) as an immunogen. Mouse B cells are immunized with this protein and then fused with myeloma cells to create hybridomas. Hybridoma cell lines producing the desired SLN antibody are screened and selected for culture in the mouse abdominal cavity. The SLN monoclonal antibody is then purified from the mouse ascites using protein G affinity chromatography, resulting in a purity exceeding 95%. This unconjugated IgG2b antibody is suitable for detecting the human SLN protein in ELISA, WB, IF, and FC applications.

Sarcolipin (SLN) is a small peptide that regulates the activity of the sarco/endoplasmic reticulum Ca²⁺-ATPase (SERCA) pump in skeletal muscle cells. Specifically, sarcolipin inhibits the activity of SERCA, leading to reduced uptake of calcium ions into the sarcoplasmic reticulum and slower muscle relaxation. This plays a crucial role in regulating the contractility of skeletal muscle cells and, consequently, overall muscle function. Dysfunction or deficiency of sarcolipin has been linked to muscle disorders such as skeletal muscle weakness and heart failure.

The MERTNL monoclonal antibody is produced using recombinant human MERTNL protein (amino acids 46-311) as the immunogen to immunize mice. B cells are isolated from the immunized mice and fused with myeloma cells to generate hybridoma cells. These hybridoma cells are screened to identify the specific cell line that secretes the MERTNL antibody. The selected hybridoma cell line is injected into the mouse abdominal cavity. The MERTNL monoclonal antibody is then purified from the mouse ascites using protein A affinity chromatography, achieving a purity exceeding 95%. This unconjugated IgG2a antibody specifically recognizes human MERTNL protein and is suitable for applications such as ELISA, IHC, and FC.

MERTNL is a protein that acts as a ligand for the MER receptor tyrosine kinase, a member of the TAM family of receptor tyrosine kinases. These kinases play critical roles in regulating immune responses, inflammation, and maintaining homeostasis. MERTNL is predominantly expressed in the placenta and has been implicated in regulating placental development and function.