The synthesis of the CA1 recombinant monoclonal antibody involves a carefully structured process. It all starts with in vitro cloning, where genes encoding both CA1 antibody's heavy and light chains are seamlessly integrated into expression vectors. Following this, these expression vectors are introduced into host cells, allowing for the recombinant antibody's expression within a cell culture environment. After expression, the CA1 recombinant monoclonal antibody is meticulously purified from the supernatant of transfected host cell lines, utilizing an affinity-chromatography purification method. An outstanding feature of this antibody is its specific reactivity with the human CA1 protein. Additionally, its versatility is highlighted, as it is suitable for a diverse range of applications, including ELISA, WB, IHC, and FC.

Carbonic anhydrase 1 (CA1) mainly catalyzes the reversible conversion of carbon dioxide (CO₂) and water (H₂O) into bicarbonate ions (HCO3^-) and protons (H₊). It is crucial for maintaining the body's acid-base balance, facilitating gas transport, and supporting various physiological processes related to pH regulation and metabolism.

The GFAP recombinant monoclonal antibody is produced through a comprehensive process that includes in vitro cloning, where genes for both the heavy and light chains of the GFAP antibody are inserted into expression vectors. These recombinant vectors are subsequently transfected into host cells to enable the recombinant expression of the antibody in a cell culture setting. After expression, the GFAP recombinant monoclonal antibody is purified from the supernatant of transfected host cell lines using affinity chromatography. This purified antibody demonstrates specific reactivity with the human GFAP protein and exhibits versatility by being suitable for ELISA and FC applications.

GFAP is primarily associated with astrocyte function and is essential for the structural support, morphology, and various roles of astrocytes in the central nervous system. It contributes to the maintenance of the blood-brain barrier, ion and water homeostasis, neurotransmitter uptake, and neuroprotection. Additionally, GFAP expression increases during reactive gliosis in response to CNS injuries or diseases, where it plays a role in glial scar formation and the brain's response to damage.

The ATP2A2 recombinant monoclonal antibody is meticulously produced through a series of steps. It all begins with in vitro cloning, where the genes responsible for both the heavy and light chains of the ATP2A2 antibody are seamlessly integrated into expression vectors. Following this, the expression vectors are introduced into host cells, allowing for the recombinant antibody's expression within a cell culture environment. Post-expression, the ATP2A2 recombinant monoclonal antibody is subjected to a stringent purification process, drawing on the capabilities of affinity chromatography for this purpose. A remarkable feature of this antibody is its specific reactivity with the human ATP2A2 protein. Furthermore, it showcases its versatility in various applications, including ELISA, IHC, IF, and FC.

ATP2A2 is an important calcium transporter protein found in the sarcoplasmic reticulum of muscle cells and the endoplasmic reticulum of skin cells. Its primary function is to regulate calcium ion concentrations within these cellular compartments, which, in turn, influences muscle contraction, skin barrier formation, calcium signaling, wound healing, and tissue homeostasis.

The GRIA2/GRIA3 recombinant monoclonal antibody is a highly specific antibody that can target two closely related proteins GRIA2 and GRIA3. It is engineered using advanced biotechnological techniques, such as genetic engineering and antibody engineering. It is produced through the cloning of specific DNA sequences encoding the GRIA2/GRIA3 antibody heavy and light chains into a plasmid vector and subsequent transfection of the recombinant vector into a host cell for expression. The resulting GRIA2/GRIA3 recombinant monoclonal antibody is purified from affinity chromatography from the cell culture supernatant. It has been validated to detect human GRIA2 and GRIA3 in ELISA and IF applications.

The production of the GSN recombinant monoclonal antibody encompasses several sequential steps, starting with in vitro cloning. In this initial phase, the genes encoding both the heavy and light chains of the GSN antibody are integrated into expression vectors. Subsequently, the expression vectors are transfected into host cells, facilitating the recombinant antibody's expression within a cell culture environment. After expression, the GSN recombinant monoclonal antibody is meticulously purified from the supernatant of transfected host cell lines, employing an affinity-chromatography purification method. Importantly, this antibody demonstrates specific reactivity with the human GSN protein and boasts versatility in three applications, including ELISA, IF, and FC.

Gelsolin (GSN) is a multifunctional protein that plays a central role in regulating the actin cytoskeleton's dynamics. Its actions on actin filaments are crucial for controlling cell shape, motility, and various cellular processes involved in normal physiology and pathological conditions.

The SMARCA4 recombinant monoclonal antibody is produced by in vitro cloning. Genes for the heavy and light chains of the SMARCA4 antibody are inserted into expression vectors that are transfected into the host cell for recombinant expression in cell culture. The SMARCA4 recombinant monoclonal antibody is purified from the tissue culture supernatant of transfected host cell lines through affinity chromatography. It can react with human SMARCA4 protein and is suitable for ELISA, IHC, IF, and FC applications.

SMARCA4 is a key component of the SWI/SNF chromatin-remodeling complex, and its primary function is to regulate gene expression by modifying chromatin structure. This activity has wide-ranging implications for cell differentiation, development, cancer suppression, DNA repair, and various other biological processes in both normal and disease states.

Through in vitro expression systems, the DEFB1 recombinant monoclonal antibody is synthesized by cloning the DNA sequences of DEFB1 antibodies sourced from immunoreactive rabbits. The immunogen employed in this process is a synthesized peptide derived from the human DEFB1 protein. The genes encoding the DEFB1 antibodies are subsequently inserted into plasmid vectors, and these recombinant plasmid vectors are transfected into host cells for antibody expression. After expression, the DEFB1 recombinant monoclonal antibody is subjected to affinity-chromatography purification and is extensively tested for functionality in ELISA and FC applications, demonstrating reactivity with the human DEFB1 protein during these assessments.

DEFB1 is an antimicrobial peptide that plays a critical role in the innate immune response by defending against a wide range of microbial pathogens. Its presence at mucosal surfaces and its broad-spectrum antimicrobial activity make DEFB1 an essential component of the body's defense against infections, particularly at sites exposed to the external environment.

In the production of the GPI recombinant monoclonal antibody, in vitro expression systems are employed, involving the cloning of DNA sequences of GPI antibodies obtained from immunoreactive rabbits. The immunogen used is a synthesized peptide derived from the human GPI protein. Subsequently, the genes encoding the GPI antibodies are inserted into plasmid vectors, and these recombinant plasmid vectors are then transfected into host cells to enable antibody expression. Following expression, the GPI recombinant monoclonal antibody undergoes affinity-chromatography purification and is extensively tested for functionality in ELISA, WB, IHC, and FC applications, demonstrating reactivity with the human GPI protein during these assessments.

Glucose-6-phosphate isomerase (GPI) plays a pivotal role in glucose metabolism, particularly in the glycolytic pathway. GPI catalyzes the conversion of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), facilitating the breakdown of glucose for energy production and contributing to glucose homeostasis. Additionally, GPI participates in the pentose phosphate pathway, which has roles in nucleotide synthesis and redox balance.

The CEACAM8 recombinant monoclonal antibody production process is initiated with in vitro cloning, wherein genes for both the heavy and light chains of the CEACAM8 antibody are integrated into expression vectors. These vectors are subsequently introduced into host cells, enabling the recombinant antibody's expression within a cell culture setting. Following expression, the CEACAM8 recombinant monoclonal antibody is meticulously purified from the supernatant of transfected host cell lines using affinity chromatography. Significantly, this antibody exhibits remarkable specificity in its binding to the human CEACAM8 protein and is highly versatile and suitable for ELISA and FC applications.

CEACAM8 is a cell surface receptor primarily found on neutrophils, and its main function is to facilitate the adhesion, migration, and transendothelial passage of neutrophils during the immune response. CEACAM8 is essential for the recruitment of neutrophils to sites of infection or inflammation, where they play a vital role in defending the body against microbial pathogens and contributing to the inflammatory response.

The synthesis of the DARC recombinant monoclonal antibody involves a stepwise procedure, commencing with in vitro cloning. This initial step entails the integration of genes encoding both the heavy and light chains of the DARC antibody into expression vectors. Subsequently, the constructed expression vectors are introduced into host cells, facilitating the recombinant antibody's expression within a cell culture environment. After this expression, the DARC recombinant monoclonal antibody is isolated from the supernatant of transfected host cell lines through the utilization of affinity chromatography for purification. Noteworthy is its specific binding capacity to the human DARC protein, as well as its remarkable versatility for ELISA and FC applications.

DARC is a cell surface receptor that binds to specific chemokines, regulating leukocyte trafficking and immune responses. Its ability to sequester chemokines in the bloodstream has implications for inflammation and immunity. Additionally, DARC is known for its involvement in blood group determination and its association with resistance to certain types of malaria.