Description

Nori Porcine S100A11 ELISA Kit Summary

Alternative names for S100A11: S100 calcium-binding protein A11, S100-A11, calgizzarin or S100C

Alternative name for porcine: Pig

Standard Curve

Kit Components
1. Pre-coated 96-well Microplate
2. Biotinylated Detection Antibody
3. Streptavidin-HRP Conjugate
4. Lyophilized Standards
5. TMB One-Step Substrate
6. Stop Solution
7. 20 x PBS
8. Assay Buffer

Other Materials Required but not Provided:
1. Microplate Reader capable of measuring absorption at 450 nm
2. Log-log graph paper or computer and software for ELISA data analysis
3. Precision pipettes (1-1000 µl)
4. Multi-channel pipettes (300 µl)
5. Distilled or deionized water

Protocol Outline
1. Prepare all reagents, samples and standards as instructed in the datasheet.
2. Add 100 µl of Standard or samples to each well and incubate 1 h at RT.
3. Add 100 µl of Working Detection Antibody to each well and incubate 1 h at RT.
4. Add 100 µl of Working Streptavidin-HRP to each well and incubate 20 min at RT.
5. Add 100 µl of Substrate to each well and incubate 5-30 min at RT.
6. Add 50 µl of Stop Solution to each well and read at 450 nm immediately.

Background: 

S100 calcium-binding protein A11 (S100A11) is a protein that is encoded by the S100A11 gene. S100A11 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A11, also known as calgizzarin or 100C, is a small acidic protein. Usually, S100A11 is in homodimeres, but it has been shown  that S100A11 heterodimerizes with S100B^[1] and it also interacts with Nucleolin,^[2] and RAD54B.^[3] The protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis. S100A11 is highly expressed in many tissues.^[4] This protein is normally found strictly in the nucleus, but appears in the cytoplasm in cancer cells. S100A11 was localized in the cytoplasm of resting human keratinocytes in vitro.^[5] S100A11 is implicated in membrane and cytoskeletar dynamics, vesicular transportation and processes of endo and exocytosis. S100A11 may interact with many cytoskeletal structures.^[5] S100A11 is able to control reorganization of actin and it is important in forming protrusion by metastatic cells. S100A11 interacts with the RAGE receptor, which is also a receptor for other S100 proteins. It lacks enzymatic activity, but regulates activity of other enzymes and functions by binding to other proteins.^[6] It is associated with cell cycle, growth, survival and apoptosis. It has been identified as dual growth mediator. Suppression of S100A11 by small interfering RNA caused cells to apoptosis, and overexpression of S100A11 has been found to inhibit apoptosis in tumor cells. Furthermore, the knock-down of S100A11 via siRNA reduces the sister-chromatid exchange and the viability of cells. IL-8 and TNF-alpha induce the expression and release of S100A11 in chondrocytes in culture and exogenous S100A11 causes chondrocyte hypertrophy. S100A11 could play a role in maintaining low-grade inflammation in osteoarthritis and in its progression.^[7] It is associated with many different types of cancers. Its overproduction has been found, for example, in breast, pancreas or colectal carcinoma and its levels can be used as clinical marker in these diseases.^[5] S100A11 enhances the recombination activity of human RAD51 in vitro. A knock-down leads to diffuse distribution of RAD54B, suggesting a potential role of S100A11 in the process of homologous recombination repair of double-strand breaks.^[8]

References

1. Deloulme JC, et al. (2000). The Journal of Biological Chemistry. 275(45): 35302–10.
2. Sakaguchi M, et al. (2003). The Journal of Cell Biology. 163(4): 825–35.
3. Murzik U, et al. (2008). Molecular Biology of the Cell. 19(7): 2926–35.
4. Inada H, et al. (1999). Biochemical and Biophysical Research Communications. 263(1): 135–8.
5. Sakaguchi M, Huh NH (2011). Amino Acids. 41(4): 797–807.
6. Zhao XQ, et al. (2000). Biochemical and Biophysical Research Communications. 267(1): 77–9.
7. Cecil DL, Terkeltaub R (2008). Journal of Immunology. 180(12): 8378–85.
8. Foertsch F, et al. (2016). Cell Cycle. 15(20): 2766–79.

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