CUSABIO cloned the DNA sequence encoding the phospho-RPA2 (T21) monoclonal antibody into the plasmid and then transfected into the cell line for expression. The monoclonal antibody was produced by immunizing the animals with the phosphopeptide corresponding to the residues surrounding Thr 21 of human RPA2. The product was purified through the affinity-chromatography method and then got the recombinant phospho-RPA2 (T21) monoclonal antibody. It belongs to the rabbit IgG. This phospho-RPA2 (T21) antibody can be used to detect human pT21-RPA2 protein in ELISA and IF applications.

RPA2 is a subunit of RPA, which is a heterotrimeric protein complex that specifically binds to ssDNA. RPA is essential for DNA replication initiation and replication elongation. When the ATR-dependent phosphorylation sites in RPA2 are mutated, the down-regulation of DNA synthesis after UV radiation is disrupted, but ATR activation is unaffected. The UV-induced, ATR-mediated inhibition of DNA replication is specifically required for Thr 21 and Ser 33, two residues among numerous phosphorylation sites in the amino terminus of RPA2.

To produce a recombinant monoclonal antibody against COL17A1, CUSABIO initiated the process by immunizing a rabbit with a synthesized peptide corresponding to the human COL17A1 protein. Subsequent steps involved isolating B cells from the rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was employed as a template for amplifying COL17A1 antibody genes using degenerate primers. These amplified COL17A1 antibody genes were then integrated into a plasmid vector and introduced into host cells for expression. The COL17A1 recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and evaluated for its utility in ELISA and WB applications, with specificity demonstrated for human COL17A1 protein.

COL17A1 is a critical structural protein that contributes to the stability of the skin and mucous membranes. Its role in anchoring the epidermis to the basement membrane, mediating cell-ECM adhesion, and maintaining the epidermal barrier is essential for the structural integrity and function of these tissues.

The synthesized DNA sequence corresponding to the pS127-YAP1 monoclonal antibody was cloned into the plasmid and then transfected into the cell line for expression. The product was purified through the affinity-chromatography method and obtained the specifically phosphorylated YAP1 recombinant monoclonal antibody. This anti-S127-YAP1 recombinant antibody is a rabbit IgG and has been tested in scientific applications, including ELISA, WB, and IHC. It only reacts with human YAP1 phosphorylated at Ser 127 residue.

The transcriptional coactivator YAP1 is involved in cell proliferation, cell-cell interactions, organ size, and tumorigenesis. YAP1's nuclear activity is dependent on post-transcriptional changes and nuclear translocation. Androgen reduces Androgen attenuates the inactivating phospho–Ser-127 modification of YAP1 and promotes YAP1 nuclear abundance and activity. The traditional Hippo kinase cascade is known to phosphorylate YAP1 at Ser127, which is required for its cytoplasmic localization and inactivation.

CUSABIO's strategy for generating a recombinant monoclonal antibody targeting CAV1 commenced with the immunization of a rabbit using a synthesized peptide from human CAV1. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which was employed as a template to extend CAV1 antibody genes using degenerate primers. These extended CAV1 antibody genes were then introduced into a plasmid vector and transfected into host cells for expression. The CAV1 recombinant monoclonal antibody was purified from the cell culture supernatant through affinity chromatography and subjected to ELISA, WB, and FC applications. It displays specific reactivity with human CAV1 protein.

CAV1 is a structural protein that oligomerizes to form caveolin complexes, which are essential for shaping and stabilizing caveolae on the cell membrane. Caveolae and CAV1 are implicated in lipid transport and metabolism, particularly in regulating lipid droplet formation, lipid uptake, and cholesterol trafficking. CAV1 has been associated with various cellular responses to stress, including oxidative stress, mechanical stress, and cellular damage. It can play a protective role in some instances.

The rabbit IgG recombinant phospho-JAK2 (Y1007 + Y1008) monoclonal antibody specifically targets the human JAK2 phosphorylated at Tyr 1007 and Tyr 1008 residues. The DNA encoding the phospho-JAK2 (Y1007 + Y1008) monoclonal antibody was inserted into the plasmid and subsequently transfected into the cell line for expression. The product was purified through the affinity-chromatography method to get the phospho-JAK2 (Y1007 + Y1008) recombinant antibody. This phospho-JAK2 (Y1007 + Y1008) antibody shows reactivity with human samples. It has been validated for multiple applications, including ELISA, WB, IHC, and IP.

JAK2 is a non-receptor protein tyrosine kinase that belongs to the Janus kinase (JAKs) family, which also includes JAK1, JAK3, and TYK2. JAKs are cytoplasmic signaling components of cytokine receptors that are activated by cytokine-mediated trans-phosphorylation, which leads to receptor phosphorylation and recruitment and phosphorylation of STAT proteins. During cytokine stimulation, JAK2 is phosphorylated on multiple sites, including Tyr 1007 and Tyr 1008.

A recombinant monoclonal antibody against PNPLA2 was generated through a series of steps, beginning with the immunization of a rabbit using a synthesized peptide derived from human PNPLA2 protein. Subsequently, B cells were isolated from the immunized rabbit, and RNA was extracted from these cells. The extracted RNA was reverse-transcribed into cDNA, which served as a template for extending PNPLA21 antibody genes using degenerate primers. These engineered PNPLA2 antibody genes were incorporated into a plasmid vector and introduced into host cells for expression. The PNPLA2 recombinant monoclonal antibody was then isolated from the cell culture supernatant via affinity chromatography and assessed for its suitability in ELISA and FC applications. It only recognizes human PNPLA2 protein.

PNPLA2/ATGL is a key enzyme involved in the hydrolysis of stored triglycerides, contributing to energy homeostasis, lipid metabolism, and the regulation of adipose tissue function. Its activity is tightly regulated and plays a crucial role in maintaining metabolic health.

This phosphorylated SMAD5 antibody CSB-RA859108A463phHU is a recombinant monoclonal antibody produced from the expression of the plasmids that were integrated by the phospho-SMAD5 (S463+S465) monoclonal antibody DNA sequence in cell lines. The phospho-SMAD5 (S463+S465) monoclonal antibody was generated from splenocytes isolated from the animals that were immunized with the human phospho-SMAD5 (S463+S465). The phospho-SMAD5 (S463+S465) recombinant antibody is a rabbit IgG antibody. It underwent purification using the affinity-chromatography method. It can detect the human phospho-SMAD5 (S463+S465). And it is suitable for ELISA and IHC analyses.

SMAD5 is a receptor-activated Smad that serves as an intracellular signal transducer for the transforming growth factor (TGF) superfamily. SMAD5 regulates cytoplasmic metabolic machinery and works as an intracellular pH messenger to maintain cell bioenergetic balance. SMAD5 is a negative regulator of embryonic hematopoiesis in a haploinsufficiency form, according to a recent study by Bing Liu et al., which helps to understand the cytogenetic mechanism by which SMAD5 serves as a leukemia suppressor.

CUSABIO designed the vector clones for the expression of a recombinant MAP2K1 antibody in mammalian cells. The vector clones were obtained by inserting the MAP2K1 antibody heavy and light chains into the plasma vectors. The recombinant MAP2K1 antibody was purified from the culture medium through affinity-chromatography. It can be used to detect MAP2K1 protein from Human in the ELISA, WB.

The phospho-MAP2K1 (T292) antibody can detect the MAP2K1 only when phosphorylated at T292. MAP2K1, also called MEK1, functions immediately upstream of MAPK in the MAPK signaling pathway. Phosphorylation of T292 on MAP2K1 by activated ERK is required for the formation of ternary complex PTEN/MAGI1/MAP2K1. MAP2K1 mutations have been found in several human malignancies, particularly melanoma, hairy cell leukemia, and lung adenocarcinoma.

CUSABIO's approach to developing a recombinant monoclonal antibody against CREB1 commenced with the immunization of a rabbit using a synthesized peptide from human CREB1 protein. B cells were subsequently isolated from the immunized rabbit, and RNA was extracted from these B cells. The extracted RNA was reverse-transcribed into cDNA, which served as a template for extending CREB1 antibody genes using degenerate primers. The engineered CREB1 antibody genes were incorporated into a plasmid vector and transfected into host cells for expression. The resulting CREB1 recombinant monoclonal antibody was then purified from the cell culture supernatant using affinity chromatography. Its suitability for ELISA, WB, and FC applications was confirmed, demonstrating specific reactivity with CREB1 proteins from human, mouse, and rat species.

CREB1 is a crucial transcription factor that regulates gene expression in response to a wide range of signals and stimuli. Its roles extend to various physiological processes, including learning and memory, cell growth and differentiation, metabolism, and the cellular response to stress.

The phospho-AKT1 (T450) recombinant monoclonal antibody is generated through a combination of protein technology and DNA recombinant techniques. First, an animal is immunized with a synthetic peptide derived from human phospho-AKT1 (T450), resulting in the production of B cells. Phospho-AKT1 (T450) antibody-producing B cells are selected and subjected to single clone identification. The genes encoding the phospho-AKT1 (T450) antibody are amplified using PCR and inserted into a plasmid vector to create a recombinant vector. This vector is introduced into host cells for antibody expression. The phospho-AKT1 (T450) recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. It only reacts with human AKT1 phosphorylated at T450 residue. Stringent validation procedures ensure its accuracy and suitability for ELISA and WB applications.