HSP27 ELISA Pair Set, Human ELISA Pair Set

Fängerantikörper 1.0 mg/mL of rabbit anti-HSP27 monoclonal antibody, Dilute to a working concentration of 1 μg/mL in CBS before coating.

Nachweisantikörper 0.5 mg/mL mouse anti-HSP27 monoclonal antibody conjugated to horseradish-peroxidase (HRP). Dilute to working concentration of 0.25 μg/mL in detection antibody diluteion buffer before use.

Standard Each vial contains 13 ng of recombinant HSP27. Reconstitute with 1 mL detection antibody dilution buffer. After reconstitution, store at -20℃ to -70℃ in a manual defrost freezer. A seven-point standard curve usi ng 2-fold serial dilutions in sample dilution buffer, and a high standard of 0.6 ng/mL is recommended.

The minimum detectable dose of Human HSP27 was determined to be approximately 9.4 pg/ml. This is defined as at least three times standard deviations above the mean optical density of 10 replicates of the zero standard.

The Human HSP27 ELISA Pair Set is for the quantitative determination of Human HSP27.

This ELISA Pair Set contains the basic components required for the development of sandwich ELISAs.

The Sino Biological ELISA Pair Set is a solid phase sandwich ELISA (Enzyme-Linked Immunosorbent Assay). It utilizes a monoclonal antibody specific for HSP27 coated on a 96-well plate. Standards and samples are added to the wells, and any HSP27 present binds to the immobilized antibody. The wells are washed and a horseradish peroxidase conjugated mouse anti-HSP27 monoclonal antibody is then added, producing an antibody-antigen-antibody "sandwich". The wells are again washed and TMB substrate solution is loaded, which produces color in proportion to the amount of HSP27 present in the sample. To end the enzyme reaction, the stop solution is added and absorbances of the microwell are read at 450 nm.

Speicherung - Detection Antibody should be protected from prolonged exposure to light. Aliquot the reagents and store at -20℃ to -70℃ in a manual defrost freezer.

Heat shock proteins (HSPs) are a group of highly conserved stress response proteins which primarily function as molecular chaperones, and are involved in a variety of biological processes including thermotolerance, inhibition of apoptosis, regulation of cell development and cell differentiation, as well as signal transduction. As a member of the chaperones, HSP27 appears in many cell types, especially all types of muscle cells, and is suggested to play an essential role in the differentiation of tissues. HSP27 has a characteristic and highly conserved amino acid sequence at the C-terminus, the so-called α-crystallin-domain which is important for the formation of stable dimers, and it is demonstrated that the oligomerization status is connected with the chaperone activity. HSP27 is also identified as an anti-apoptotic molecule. It interacts with the outer mitochondrial membranes and interferes with the activation of cytochrome c/Apaf-1/dATP complex and therefore inhibits the activation of procaspase-9 and procaspase-3. Furthermore, HSP27 also exerts functions in protecting actin filaments from fragmentation and the activation of the certain proteasome.