27727 Results for: "affinity chromatography"

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled IgG covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy and light chains of rabbit IgG, and with the light chains of rabbit IgM and IgA. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rat, sheep, and chicken serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using mouse IgM covalently linked to agarose beads. Based on ELISA and/or flow cytometry, this antibody reacts with the heavy chain of mouse IgM. This antibody was tested by Dot Blot and/or solid phase adsorbed for minimal cross-reactivity with mouse IgG1, IgG2a, IgG3, and IgA, pooled human sera and purified human paraproteins. The conjugate has been specifically tested and qualified for Western blot. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using goat IgG covalently linked to agarose beads. Based on ELISA, this antibody reacts with the heavy and light chains of goat IgG and sheep IgG. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rabbit, rat, chicken, guinea pig, hamster, swine, and horse serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled IgG covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy and light chains of rabbit IgG, and with the light chains of rabbit IgM and IgA. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rat, sheep, and chicken serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Li-Cor

The antibody was isolated from antisera by affinity chromatography using antigens coupled to agarose beads. Based on ELISA, the antibody reacts with the heavy and light chains on mouse IgG and with the light chains of mouse IgM and IgA. This antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reactivity with bovine, chicken, goat, guinea pig, horse, human, rabbit, and sheep serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using mouse IgG2a covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy chain of mouse IgG2a. This antibody was tested by Dot Blot and/or solid phase adsorbed for minimal cross-reactivity with mouse IgM, IgG1, IgG2b, IgG3, IgA, pooled human sera, and purified human paraproteins. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, virus titration assay, FRET-based assays, and small animal imaging.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled IgG covalently linked to agarose. Based on ELISA and flow cytometry, this antibody reacts with the heavy and light chains of rabbit IgG, and with the light chains of rabbit IgM and IgA. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rat, sheep, and chicken serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, and small animal imaging.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using mouse IgG1 covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy chain of mouse IgG1. This antibody was tested by Dot Blot and/or solid phase adsorbed for minimal cross-reactivity with mouse IgM, IgG2a, IgG2b, IgG3, and IgA, pooled human sera and purified human paraproteins. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, virus titration assay, FRET-based assays, and small animal imaging.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled IgG covalently linked to agarose. Based on ELISA, this antibody reacts with the heavy and light chains of goat IgG and with sheep IgG. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rabbit, rat, chicken, guinea pig, hamster, swine, and horse serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, and small animal imaging.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using mouse IgG2b covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy chain of mouse IgG2b. This antibody was tested by Dot Blot and/or solid phase adsorbed for minimal cross-reactivity with mouse IgM, IgG1, IgG2a, IgG3, IgA, pooled human sera, and purified human paraproteins. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, virus titration assay, FRET-based assays, and small animal imaging.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using mouse IgM covalently linked to agarose beads. Based on ELISA and/or flow cytometry, this antibody reacts with the heavy chain of mouse IgM. This antibody was tested by Dot Blot and/or solid phase adsorbed for minimal cross-reactivity with mouse IgG1, IgG2a, IgG3, and IgA, pooled human sera and purified human paraproteins. The conjugate has been specifically tested and qualified for Western blot. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using goat IgG covalently linked to agarose beads. Based on ELISA, this antibody reacts with the heavy and light chains of goat IgG and sheep IgG. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rabbit, rat, chicken, guinea pig, hamster, swine, and horse serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Proteintech

Mitochondrial transcription termination factor （MTERF）also named as Mterf1 is a 399 amino acid protein, which localizes in the mitochondrion and belongs to the mTERF family. MTERF contains three leucine zippers that form a three-stranded coiled-coil that binds to DNA. It has been suggested that only the phosphorylated form of MTERF has transcription termination activity. MTERF plays a central role in the control of mitochondrial rRNA and mRNA synthesis. MTERFD1 is also thought to act as a mitochondrial transcription regulator and is expressed as two isoforms produced by alternative splicing.Using DNA affinity chromatography, a fraction called MTERF was found to be associated with foot-printing capacity, and this contained two polypeptides of 34 and 31 kDa. Moreover, termination-promoting activity appears to reside in the 34-kDa protein. .

Supplier: Proteintech

Protein tags are protein or peptide sequences located either on the C- or N- terminal of the target protein, which facilitates one or several of the following characteristics: solubility, detection, purification, localization and expression. Maltose binding protein(MBP) is the 370 amino acid product of the E.coli mal E gene. MBP is a useful affinity tag that can increase the expression level and solubility of the resulting tagged protein. The MBP tag also promotes proper folding of the attached protein. Plasmid vectors have been constructed utilizing the MBP domain that allow the synthesis of high levels of MBP-fusion proteins that can be purified in a one step procedure by affinity chromatography cross linked amylose resin. Once bound to amylose, the MBP protein can then be separated from the target protein by cleavage by coagulation Factor Xa at a specific four residue site. Alternatively, the intact fusion protein can be specifically eluted from the resin by the addition of excess free maltose. Subsequent to elution, MBP fusion protein can be visualized either by Western blot analysis or immunoprecipitation using antibodies specific for the MBP-tag. An antibody to MBP can also be used to isolate or detect expression of the protein.

Supplier: Li-Cor

The antibody was isolated from antisera by affinity chromatography using antigens coupled to agarose beads. Based on ELISA, the antibody reacts with the heavy and light chains on mouse IgG and with the light chains of mouse IgM and IgA. This antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reactivity with bovine, chicken, goat, guinea pig, horse, human, rabbit, and sheep serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled IgG covalently linked to agarose. Based on ELISA, this antibody reacts with the heavy and light chains of goat IgG and with sheep IgG. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, mouse, rabbit, rat, chicken, guinea pig, hamster, swine, and horse serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, and small animal imaging.

Supplier: Bioss

The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Supplier: Anaspec

Renin, a highly specific aspartyl protease, cleaves angiotensinogen, produced in the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE (Angiotensin Converting Enzyme). Angiotensin II constricts blood vessels, leading to increased blood pressure. It also increases the secretion of ADH and aldosterone, and stimulates the hypothalamus to activate the thirst reflex. Since an overactive renin-angiotensin system leads to hypertension, renin is proposed as a therapeutic target for this disease

The recombinant human pro-renin was expressed in HEK cells and converted to the active renin. After affinity chromatography, the active enzyme has a purity of >99% by SDS-PAGE. The molecular mass of active human renin is approximately 40 kDa.
The activity of enzyme can be measured in FRET-based assays

Supplier: Bioss

This antibody reacts with Escherichia coli HD5a (E.coli HD5a), Escherichia coli is a gram-negative bacillus that belongs to a larger group of Enterobacteriae - bacteria that inhabit the gastrointestinal tract. Although usually a harmless resident of the gut, some strains have the potential to cause serious problems, especially where there is an immature immune system or immunosuppression, or where the subtype of organism has acquired the ability to produce pathogenic toxins. E. coli DH5_ strain is an engineering strain widely used in biopharmaceuticals. According to the requirements of product quality inspection, it is necessary to detect the residual amount of DH5_ bacterial protein in biological products. This product is an anti-serum obtained by immunizing rabbits with DH5_ bacterial protein as an antigen, and purified by affinity chromatography to obtain antibody IgG, which can be used for ELISA, Western Blot and other experimental tests.

Supplier: Bioss

This antibody reacts with Escherichia coli HD5a (E.coli HD5a), Escherichia coli is a gram-negative bacillus that belongs to a larger group of Enterobacteriae - bacteria that inhabit the gastrointestinal tract. Although usually a harmless resident of the gut, some strains have the potential to cause serious problems, especially where there is an immature immune system or immunosuppression, or where the subtype of organism has acquired the ability to produce pathogenic toxins. E. coli DH5_ strain is an engineering strain widely used in biopharmaceuticals. According to the requirements of product quality inspection, it is necessary to detect the residual amount of DH5_ bacterial protein in biological products. This product is an anti-serum obtained by immunizing rabbits with DH5_ bacterial protein as an antigen, and purified by affinity chromatography to obtain antibody IgG, which can be used for ELISA, Western Blot and other experimental tests.

Supplier: Li-Cor

Isolation of specific antibodies was accomplished by affinity chromatography using pooled mouse IgG covalently linked to agarose beads. Based on ELISA and flow cytometry, this antibody reacts with the heavy and light chains of mouse IgG1, IgG2a, IgG2b, and IgG3, and with the light chains of mouse IgM and IgA. This antibody was tested by Dot Blot and/or solid-phase adsorbed for minimal cross-reactivity with human, rabbit, goat, rat, and horse serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot and In-Cell Western™ assay applications. Highly Recommended for: Western blot, In-Cell Western Assay, On-Cell Western Assay, protein array, immunohistochemistry, microsciopy, 2D gel detection, tissue section imaging, and small animal imaging.

Supplier: Li-Cor

The antibody was purified from antisera by affinity chromatography using antigens coupled to agarose beads. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule rat IgG and with the light chains of other rat immunoglobulins. No reactivity was detected against non-immunoglobulin serum proteins. This antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reactivity with mouse, bovine, horse, human, and rabbit serum proteins, but may cross-react with immunoglobulins from other species. The conjugate has been specifically tested and qualified for Western blot applications. Recommended for: Western blot, proein array, immunohistochemistry, microscopy, 2D gel detection, and tissue section imaging. NOT RECOMMENDED for: small animal imaging, In-Cell Wesern assays, or On-Cell Western assays.