The GAPDH Monoclonal Antibody is a specific antibody that targets GAPDH. The GAPDH antibody is an internal reference antibody that functions as a loading control to ensure equal protein loading and accurate quantification of protein expression levels in different samples. This antibody can detect GAPDH in human, mouse, and rabbit species.
The immunogen used to generate this GAPDH antibody is the 2-335 amino acid region of recombinant Human GAPDH protein. The GAPDH Monoclonal Antibody is raised in mouse and belongs to the IgG1 isotype. It is purified using Protein G and reaches a purity level of greater than 95%.
The GAPDH Monoclonal Antibody is available in liquid form and has been tested in various applications, including ELISA, WB, IHC, IP, and IF. These applications make the antibody a versatile tool for the detection and analysis of GAPDH in different contexts.
Moreover, the GAPDH Monoclonal Antibody has been cited in a paper by H Miao, et al. in 2022, which highlights its utility in scientific research. The use of this validated antibody in research increases the reliability of the results and ensures reproducibility.
The product CSB-MA000141M0m is an unconjugated monoclonal antibody against HA-Tag. It is derived from the mouse myeloma cell-splenocyte hybridoma. The splenocyte is screened from the mouse immunized with the HA-Tag synthetic peptide conjugated to KLH and can secret HA-Tag antibody. This HA-Tag antibody can react with HA-Tag protein from all species. It is matched with the mouse IgG2b isotype. Protein A-mediated purification of this HA-Tag antibody makes its purity up to more than 95%. This antibody has been validated for use in ELISA, WB, IP, IF, and FC applications.
The HA tag is a 9-amino acid peptide derived from the human influenza virus hemagglutinin (HA). It is widely used as a common epitope tag in expression vectors. Because the HA tag does not interfere with the bioactivity or biodistribution of the recombinant protein, it is often fused to the N-terminal or C-terminal of recombinant protein thus facilitating the detection, isolation, and purification of proteins of interest.
The monoclonal anti-E-Tag (IgG1 isotype) antibody is produced from the hybridomas fused by the myeloma cells and mouse splenocytes. The splenocytes are isolated from the mouse immunized with the E-tag synthetic peptide conjugated to KLH. This unconjugated E-Tag monoclonal antibody is purified through protein G with a purity of more than 95%. It can react with all E-Tag-fused proteins. And it is amenable to ELISA, WB, and IP applications.
E-Tag is a short amino acid sequence (GAPVPYPDPLEPR) that is frequently used as an epitope tag in molecular biology experiments to facilitate the detection and purification of recombinant proteins. The E-Tag sequence is genetically fused to the protein of interest, and antibodies or affinity resins that specifically recognize the E-Tag can be used to detect or purify the tagged protein. This allows researchers to study the expression, localization, and function of the protein in cells or tissues.
The product CSB-MA754656A0m is an unconjugated monoclonal antibody against the human TUBA1A. It is produced from the mouse splenocyte-myeloma cell fused hybridoma. The splenocyte is isolated from the mouse immunized with the synthesized peptide that is derived from human TUBA1A protein (297-309aa). This TUBA1A monoclonal antibody can react with TUBA1A protein from four species, including human, rabbit, rat, and mouse. Protein A-mediated purification of this TUBA1A monoclonal antibody makes its purity up to more than 95%. This antibody has been validated for use in ELISA, WB, IHC, IF, IP, and FC applications.
TUBA1A protein plays a crucial role in the organization and stabilization of microtubules, which are important for maintaining the shape and structural integrity of cells. Additionally, TUBA1A has been shown to play a role in neuronal development and function, as it is a major constituent of the microtubules that form the axon and dendrites of neurons. Mutations in the TUBA1A gene are associated with a range of neurological disorders, including microcephaly, lissencephaly, and intellectual disability.
This GAPDH monoclonal antibody was raised by fusion of B lymphocytes with immortal cell cultures to produce hybridomas (A Recombinant Human GAPDH protein was used in the immunization process). Hybridomas would produce many copies of GAPDH monoclonal antibody. The specificity of this GAPDH monoclonal antibody makes it extremely efficient for binding of antigen within a mixture of GAPDH. In addition, this antibody has been validated in ELISA, WB, IHC, IP, IF.
GAPDH (G3PD) is the abbreviation of glyceraldehyde-3-phosphate dehydrogenase, which is an enzyme in glycolysis and consists of 4 subunits of 30-40 kDa. The molecular weight is 146 kDa. The enzyme gene is a house-keeping gene, which is expressed at a high level in almost all tissues. The protein expression level in the same cell or tissue is generally constant and is not induced by the partial recognition sites contained. The influence of the substance remains constant, so it is widely used as a standardized internal reference for the extraction of total RNA, poly(A)+ RNA, Western blot and other experimental operations.