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The S100 protein family is a prominent subgroup within the larger group of Ca²⁺-binding EF-hand proteins. Their name, "S100," originates from their solubility in a 100% saturated ammonium sulfate solution at neutral pH, a characteristic first identified by B.W. Moore in 1965. These proteins are small, acidic, and typically range from 10 to 12 kDa in size. They are characterized by their two EF-hand motifs, four α-helical segments, a central hinge region of variable length, and variable N- and C-terminal domains.
In vertebrates, the S100 protein family is quite extensive, with at least 25 identified members. These proteins are clustered primarily at chromosome locus 1q21, known as the epidermal differentiation complex. However, they are notably absent in invertebrates.
Figure 1. Schematic of S100 protein signaling receptors. (Donato R, et al., 2013)
S100 proteins are multifunctional and exhibit a variety of cellular roles. They lack intrinsic catalytic activity and are primarily thought to act as calcium sensor proteins. Much like calmodulin and troponin C, S100 proteins undergo conformational changes upon calcium binding, which modulates their biological activity. This change involves the rearrangement of their helices to expose a cleft that forms the target protein binding site.
In addition to calcium, some S100 proteins also bind Zn²⁺ and Cu²⁺, suggesting that these metals might regulate their activity in certain contexts. For instance, S100B interacts with tau protein and can inhibit tau protein phosphorylation through protein kinase II, and Cu²⁺ binding to S100B might offer neuroprotective effects.
The diverse functions of S100 proteins arise from:
1. The broad diversification of their members (25 in humans).
2. The different metal ion-binding properties of individual S100 proteins.
3. Their spatial distribution across specific intracellular compartments or extracellular spaces.
4. Their ability to form non-covalent homo- and hetero-dimers, facilitates dynamic exchange of S100 subunits.
S100 proteins play a role in various cellular processes, including contraction, motility, cell growth and differentiation, cell cycle progression, transcription, membrane organization, cytoskeleton dynamics, protection from oxidative damage, protein phosphorylation, and secretion.
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| Cat.No. | Product Name | Price |
| CSC-SC013732 | Panoply™ Human S100A9 Over-expressing Stable Cell Line | Inquiry |
| CSC-DC013732 | Panoply™ Human S100A9 Knockdown Stable Cell Line | Inquiry |
| CLOE-0984 | Human S100A9 Insect Cell Lysate | Inquiry |
| CLKO-1941 | S100A8 KO Cell Lysate-HeLa | Inquiry |
| CSC-RT2080 | S100A8 Knockout Cell Line-HeLa | Inquiry |
| CSC-SC013731 | Panoply™ Human S100A8 Over-expressing Stable Cell Line | Inquiry |
| CSC-DC013731 | Panoply™ Human S100A8 Knockdown Stable Cell Line | Inquiry |
| CLOE-0986 | Human S100A8 Insect Cell Lysate | Inquiry |
| CSC-SC013718 | Panoply™ Human S100A1 Over-expressing Stable Cell Line | Inquiry |
| CSC-DC013718 | Panoply™ Human S100A1 Knockdown Stable Cell Line | Inquiry |
| CLOE-1647 | Human S100A1 HEK293 Cell Lysate | Inquiry |
S100 proteins have significant clinical relevance due to their involvement in several diseases. The most studied member, S100B, is known for its neurotrophic effects at physiological concentrations and neurotoxic effects at higher concentrations. It is used as a marker in various clinical disorders, including:
Traumatic Brain Injury (TBI): Elevated levels of S100B in blood and cerebrospinal fluid (CSF) after TBI can indicate brain damage. While its presence helps identify intracerebral lesions, its reliability in predicting long-term outcomes is debated. S100B's role in TBI also includes potential neuroprotective effects and promoting repair.
Alzheimer's Disease: Elevated S100B levels correlate with neurodegeneration and may contribute to disease progression.
Subarachnoid Hemorrhage: Increased S100B levels correlate with disease severity and prognosis.
Other Neurological Conditions: Elevated S100B levels are also noted in conditions like acute stroke, multiple sclerosis, systemic lupus erythematosus, and bipolar disorder.
Malignant Melanoma: S100B levels reflect tumor load and prognosis. It is used in conjunction with other markers for detecting recurrence or metastases.
Breast Cancer: High S100A4 levels are associated with poor survival rates and metastatic potential.
Various Cancers: S100 proteins, including S100A2 and S100A4, show altered expression in several cancers, serving as valuable prognostic tools. S100A2 is overexpressed in non-small cell lung cancer and other tumors, while S100A8/A9 complexes are implicated in cancer cell proliferation and metastasis.
Analytical techniques such as immunoradiometric assays (IRMA), mass spectrometry, Western blotting, ELISA, electrochemiluminescence, and quantitative PCR are used to detect changes in S100 protein levels. These methods offer high sensitivity and are crucial for clinical diagnosis and monitoring.
The S100 protein family encompasses a wide array of functions and applications. Their roles in cellular processes and diseases make them important subjects of study in both research and clinical settings. Ongoing research aims to further elucidate their functions and enhance their utility in diagnosing and treating various conditions.
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