To create the TUBB1 recombinant monoclonal antibody, the process begins with the acquisition of the TUBB1 antibody genes. These genes are then introduced into suitable host cells, where they serve as the basis for synthesizing TUBB1 antibodies utilizing a cell-based expression and translation system. This method offers several advantages, including significantly enhancing the purity and stability of the resulting TUBB1 recombinant monoclonal antibodies, as well as boosting their affinity and specificity. Following synthesis, the TUBB1 recombinant monoclonal antibody undergoes a purification step utilizing affinity chromatography. Subsequently, it undergoes thorough testing through various assays, including ELISA, IHC, and FC. This antibody exclusively recognizes the human TUBB1 protein.

TUBB1 is a critical component of microtubules, and its primary role is to contribute to the structural integrity of the cytoskeleton and participate in various cellular processes, including intracellular transport, cell division, cell motility, and intracellular organization. Dysfunction in microtubule dynamics can have significant implications for cell function and may contribute to diseases such as cancer and neurological disorders.

The vectors expressing anti-CTNNB1 antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-CTNNB1 (S33/S37), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening CTNNB1 antibody gene, and amplifying heavy and light chain sequence by PCR and cloning them into plasma vectors. After that, the vector clones were transfected into the mammalian cells for production. The product is the recombinant CTNNB1 antibody. Recombinant CTNNB1 antibody in the culture medium was purified using affinity-chromatography. It can react with CTNNB1 protein from Human and is used in the ELISA, IF.

CTNNB1 (Catenin Beta 1) is a protein-coding gene. Diseases associated with CTNNB1 include Pilomatrixoma and Neurodevelopmental Disorder with Spastic Diplegia and Visual Defects. Associated pathways include the NF-kappaB pathway and apoptotic cleavage of cellular proteins. According to some studies, CTNNB1 may have the following characteristics.
CTNNB1 mutations are highly prevalent in sporadic castrated tumors. Mutations in the β-catenin gene (CTNNB1) have recently been implicated in the pathogenesis of some colon cancers and melanomas. CTNNB1 signaling plays a key role in the development of a considerable proportion of prostate cancer. The nuclear expression of β-catenin is an accurate immunohistochemical surrogate for CTNNB1 exon 3 mutations and thus may be considered in risk stratification for endometrial cancer.

The HIST1H3A recombinant monoclonal antibody preparation is to obtain the HIST1H3A antibody genes, to introduce the HIST1H3A antibody genes into suitable host cells, and to synthesize HIST1H3A antibodies using cell expression and translation system. This method can not only greatly improve the purity and stability of the synthesized HIST1H3A recombinant monoclonal antibodies, but also increase antibodies' affinity and specificity. This HIST1H3A recombinant monoclonal antibody underwent affinity chromatography purification and was tested in ELISA, WB, IHC, and IF assays. It can recognize both human and mouse HIST1H3A protein.

HIST1H3A, also known as histone H3.1, is a critical component of chromatin, serving as a structural protein that helps package DNA and regulate gene expression. Its dynamic modifications and interactions with other proteins are essential for the intricate regulation of various cellular processes, including gene transcription, DNA replication, DNA repair, and cell division.

The vectors expressing anti-POLR2A antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-POLR2A (S2), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening POLR2A antibody gene, and amplifying heavy and light chain sequence by PCR and cloning them into plasma vectors. After that, the vector clones were transfected into the mammalian cells for production. The product is the recombinant POLR2A antibody. Recombinant POLR2A antibody in the culture medium was purified using affinity-chromatography. It can react with POLR2A protein from Human and is used in the ELISA, WB, IHC, IF, IP.

POLR2A encodes the largest subunit of RNA polymerase II, the polymerase responsible for the synthesis of eukaryotic messenger RNA. The product of POLR2A contains a carboxy-terminal domain consisting of heptapeptide repeats that is essential for polymerase activity. According to some studies, POLR2A may have the following characteristics.
Potential for pH-responsive nanoparticles and precise targeting of POLR2A in TNBC harboring common TP53 genomic alterations. The clinical consequences of a potentially pathogenic variant in POLR2A depend on its effect on pol-II-mediated transcription, as POLR2A variants predicted to cause loss of RPB1 protein are more tolerated than missense variants. BCAR1 promotes proliferation and cell growth, likely through upregulation of POLR2A and subsequent enhancement of catalytic and transferase activity. Humanized monoclonal antibody-induced nuclear localization of CD26 inhibits tumor cell growth by regulating POLR2A transcription.

The IL1R1 recombinant monoclonal antibody is generated through a multi-step process involving the acquisition of IL1R1 antibody genes, their introduction into suitable host cells, and the synthesis of IL1R1 antibodies using a cell-based expression and translation system. This approach not only enhances the purity and stability of the resulting IL1R1 recombinant monoclonal antibodies but also improves their affinity and specificity. The IL1R1 recombinant monoclonal antibody undergoes purification via affinity chromatography and is subjected to testing in both ELISA and FC assays. It is important to note that this antibody selectively recognizes the human IL1R1 protein.

IL1R1 is a receptor protein that plays a crucial role in mediating inflammatory responses and immune system activation. Its activation by IL-1 cytokines initiates a cascade of events that contribute to the body's defense against infections and the regulation of inflammation. Dysregulation of the IL-1 pathway can lead to chronic inflammatory diseases and autoimmunity.

To produce the phospho-POLR2A (S5) recombinant monoclonal antibody, the initial step entails isolating the genes encoding the POLR2A antibody from rabbits that have been previously immunized with a synthesized peptide derived from the human POLR2A protein phosphorylated at S5. Subsequently, these antibody genes are cloned into specialized expression vectors. Following this genetic modification, the vectors are introduced into host suspension cells. Following successful transfection, positive cells are cultured to promote the expression and secretion of antibodies. The phospho-POLR2A (S5) recombinant monoclonal antibody is then meticulously purified from the cell culture supernatant using affinity chromatography. Finally, the antibody's functionality is rigorously tested through a battery of assays, including ELISA, WB, IHC, and IF, confirming its ability to effectively react with human POLR2A protein phosphorylated at S5.

Phosphorylation of POLR2A at S5 is a fundamental regulatory step in eukaryotic gene expression. It helps orchestrate the complex transcriptional processes that lead to the synthesis of functional mRNA molecules, ensuring proper gene expression and cellular function. Dysregulation of this phosphorylation event can have significant implications for gene expression and is associated with various diseases and developmental disorders.

The vectors expressing anti-CREB1 antibody were constructed as follows: immunizing an animal with a synthesized peptide derived from human Phospho-CREB1 (S133), isolating the positive splenocyte and extracting RNA, obtaining DNA by reverse transcription, sequencing and screening CREB1 antibody gene, and amplifying heavy and light chain sequence by PCR and cloning them into plasma vectors. After that, the vector clones were transfected into the mammalian cells for production. The product is the recombinant CREB1 antibody. Recombinant CREB1 antibody in the culture medium was purified using affinity-chromatography. It can react with CREB1 protein from Human and is used in the ELISA, WB, IHC, IF.

In adult mammalian retina, p-CREB1 is normally limited to the ganglion cell and inner nuclear layers. It appears that as in other parts of the nervous system, stressful stimuli can induce phosphorylation of CREB1 in retinal neurons. CREB1 not only controls the expression of its own direct target genes, but is also involved in signaling crosstalk with nuclear receptors such as the glucocorticoid receptor and ERα. Whether CREB1 stimulates or represses nuclear receptor activity seems to be cell-context dependent. Upon phosphorylation of serine 133 by PKA, pCREB1 can specifically recruit the coactivator CREB binding protein (CBP) and its paralog p300. The stimulatory activity of CREB1 requires its DNA binding and activation by phosphorylation, and affects the chromatin recruitment of ERα. CREB1 and ERα are biochemically associated and share hundreds to thousands of chromatin binding sites upon stimulation by estrogen and cAMP, respectively.

The generation of the recombinant monoclonal antibody specific to CDH1 involves the initial step of inserting CDH1 antibody genes into plasmid vectors. These recombinant plasmid vectors are then introduced into appropriate host cells for expression using exogenous protein expression technology. Following this, the CDH1 recombinant monoclonal antibody is subject to purification using affinity chromatography. It has been meticulously validated for multiple applications, including ELISA, WB, and IHC. Notably, this antibody exhibits reactivity with both human and mouse CDH1 proteins.

CDH1 (E-cadherin) is a fundamental protein that governs calcium-dependent cell-cell adhesion in epithelial tissues. Its primary function is to promote tissue integrity, control cell behavior, and participate in developmental processes. Dysfunction or loss of CDH1 function can have significant implications for tissue stability and is associated with various diseases, including cancer.

The MRAS recombinant monoclonal antibody was created by integrating the MRAS antibody genes into plasmid vectors. These engineered plasmid vectors were subsequently introduced into suitable host cells using exogenous protein expression techniques, facilitating the production of the antibody. Following the production process, the MRAS recombinant monoclonal antibody underwent purification through affinity chromatography. Comprehensive validation was conducted to confirm the suitability of this MRAS recombinant monoclonal antibody for three applications, including ELISA, IHC, and IF.

The MRAS protein is a member of the Ras superfamily and functions as a molecular switch in cellular signaling pathways. Its main functions include regulating cell growth, differentiation, survival, and receptor tyrosine kinase (RTK) signaling transduction.

CUSABIO cloned MLKL antibody-coding genes into plasma vectors and then transfected these vector clones into mammalian cells using a lipid-based transfection reagent. Following transient expression, the recombinant antibodies against MLKL were harvested and characterized. The recombinant MLKL antibody was purified by affinity-chromatography from the culture medium. It can be used to detect MLKL protein from Human in the ELISA, IHC.

MLKL belongs to the protein kinase superfamily. The encoded protein contains a protein kinase-like domain. It is considered inactive because it lacks several residues required for activity. Diseases associated with MLKL include young adulthood diabetes and inflammatory bowel disease. Its related pathways include DNA damage response and regulation of c-FLIP. According to some studies, MLKL may have the following characteristics.
MLKL is a functional RIP3 substrate that binds to RIP3 through its kinase-like structure, but lacks kinase activity itself. RIP3 phosphorylates MLKL at T357 and S358. Modification of MLKL is critical for dissemination of the necrotic pathway downstream of RIPK3. Plasma membrane transport of trimeric MLKL protein is required for TNF-induced necrosis. In the absence of MLKL, RIPK3 promotes cell death and activation of the NLRP3 inflammasome. MLKL plays an important role in the necrosis of macrophages and MEFs.