FUBP1 is a DNA and RNA binding protein that mainly regulates the transcription of its target genes. FUBP1 stimulates cell proliferation, suppresses apoptosis, and enhances cell migration by regulating complex networks. FUBP1 is up-regulated in various types of cancer, including renal cell carcinoma, breast cancer, prostate cancer, and bladder cancer. Loss-of-function analyses of FUBP1 reveal its essential roles in hematopoietic stem cell maintenance and survival.

PABPN1 is a multifactorial mRNA processing regulator that controls muscle wasting and atrophy. PABPN1 activates polydenylate polymerase and regulates the length of the poly(A) tail on RNA transcripts. PABPN1 influences mRNA levels and stability by regulating the usage of alternative polyadenylation sites. PABPN1 is also involved in the processing of long non-coding RNA and short nucleolar RNA, as well as nuclear surveillance, which results in RNA hyperadenylation and degradation. PABPN1 levels in humans are lowered from midlife onwards, particularly in skeletal muscles. Oculopharyngeal muscular dystrophy (OPMD), a late-onset myopathy, is caused by an expansion mutation in PABPN1. Reduced PABPN1 levels cause muscle wasting and atrophy.

B cells were irritatingly produced with a synthetic peptide derived from human PELP1 and then fused with myeloma cells to create hybridomas. The variable light (VL) and variable heavy (VH) domains of PELP1 antibody-producing hybridomas were sequenced, which served as a blueprint for the construction of a vector for recombinant production. The PELP1 monoclonal antibody gene-carrying vector was transfected into cells, and the PELP1 recombinant monoclonal antibody was extracted and purified using affinity chromatography from the cell culture supernatant. The purified antibody was then assessed for specificity using ELISA, WB, and IHC applications and it was found to exclusively target human PELP1 protein.

The PELP1 protein plays a role in multiple cellular processes. It acts as a transcriptional co-activator, meaning that it helps to activate the expression of certain genes. It is also involved in protein-protein interactions and may help to regulate signaling pathways involved in cell growth and differentiation. In addition, PELP1 has been linked to hormone receptor signaling, with some studies suggesting that it may play a role in breast cancer development and progression.

Phospho-ATF2 (T71) recombinant monoclonal antibody was prepared by cloning the coding sequence for the phospho-ERN1 (S724) monoclonal antibody (produced by immunizing animals with the synthetic phosphopeptide of ERN1) into the plasmids and transfecting the clones into cell lines. It is a rabbit IgG purified through the affinity-chromatography method. This phospho-ATF2 (T71) antibody detects endogenous levels of human ATF2only when phosphorylated at T71. It can be applied in ELISA, WB, and IF analyses.

ATF2 is found in almost all cell types and regulates the transcription of genes involved in a wide range of biological processes, including cell growth, development, and stress. ATF2 participates in the transmission of extracellular signals to the nucleus, promoting transcriptional responses to stimuli. Many stimuli, such as growth hormones, UV radiation, and cytokines, can activate ATF2. Stress-activated protein kinases (SAPKs) (e.g., p38) phosphorylate ATF2 at Thr69 and Thr71, which activates transcriptional activation of ATF2. ATF2 can interact with other AP1 proteins and translocate to the nucleus after being phosphorylated at T69/T71, allowing it to influence gene expression.

CUSABIO put the phospho-SMC1A (S957) monoclonal antibody DNA sequence into the plasmid, which was subsequently transfected into the cell line for expression. Immunizing mice with the phosphopeptide corresponding to residues surrounding Ser 957 of human SMC1A produced the phospho-SMC1A (S957) monoclonal antibody. The recombinant phospho-SMC1A (S957) monoclonal antibody was obtained after the product was purified using affinity chromatography. It's a rabbit IgG antibody. This phospho-SMC1A (S957) antibody has undergone ELISA and WB quality testing. It can bind to the pS957-SMC1A in human samples.

SMC1A is a subunit of the evolutionarily conserved four-subunit complex cohesion. SMC1A plays an important role in genome integrity, chromosomal function, gene control, and double-stranded DNA repair, among other functions. It is phosphorylated by both ATR and ATM protein kinases and is involved in the G2/M checkpoint. SMC1A has been linked to the formation of tumors in various types of human malignancies. SMC1A promotes prostate cancer development and migration in vitro and in vivo, according to the finding of Xiu-Wu Pan et al.

The MAPK1/MAPK3 recombinant monoclonal antibody is produced using in vitro expression systems. The expression systems are developed by cloning the MAPK1/MAPK3 antibody DNA sequences from immunoreactive rabbits. The immunogen is a synthesized peptide derived from the human MAPK1/MAPK3 protein. Then, the MAPK1/MAPK3 antibody genes are inserted into plasmid vectors. The recombinant plasmid vectors are transfected into host cells for antibody expression. The MAPK1/MAPK3 recombinant monoclonal antibody undergoes affinity-chromatography purification and is tested in ELISA, WB, IHC, and FC applications. It reacts with both human and mouse MAPK1/MAPK3 proteins.

MAPK1 (ERK2) and MAPK3 (ERK1) are both serine/threonine kinases and are highly homologous and often have overlapping functions. Once activated by extracellular signals, such as growth factors, cytokines, and mitogens, MAPK1 and MAPK3 phosphorylate a variety of downstream target proteins, including transcription factors and other kinases, thus triggering cascade events that promote cell proliferation, regulate cell cycle progression, and participate in cell differentiation and survival.

The phospho-PDGFRB (Y740) recombinant monoclonal antibody is a highly specific antibody against the human pY740-PDGFRB protein. This phosphorylated PDGFRB antibody was expressed through the clone of the DNA sequence encoding the pY740-PDGFRB monoclonal antibody into plasmids and subsequent transfection into cell lines. Its isotype matches with the rabbit IgG. This anti-pY740-PDGFRB antibody can be used in ELISA and WB applications and recognizes the human PDGFRB phosphorylated at Tyr 740 residue. It has been purified through affinity-chromatography.

When PDGF binds to the PDGFRB, it causes receptor tyrosine phosphorylation and the stable interaction of several signaling molecules, including PLC-gamma, the GAP, and PI3K. PDGFB and its receptor, PDGFRB, are necessary for the development of vascular mural cells such as pericytes and vascular smooth muscle cells. Three PDGFR tyrosine phosphorylation sites in the kinase insert domain have previously been identified as critical for the stable association of GAP and PI3K. Two of them, tyrosine Y740 and Y751, are necessary for PI3K stability, whereas Y771 is required for GAP binding.