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S100B Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P-Leica, FC, E |
|---|---|
| Primary Accession | P04271 |
| Other Accession | Q6YNR6 |
| Reactivity | Human, Mouse, Rat |
| Predicted | Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 10713 Da |
| Gene ID | 6285 |
|---|---|
| Other Names | Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, S100B |
| Target/Specificity | This S100B antibody is generated from rabbits immunized with S100B recombinant protein. |
| Dilution | WB~~1:2000 IHC-P-Leica~~1:500 FC~~1:10~50 IHC~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | S100B Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | S100B {ECO:0000303|PubMed:6487634, ECO:0000312|HGNC:HGNC:10500} |
|---|---|
| Function | Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:20950652, PubMed:6487634). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer (PubMed:20950652, PubMed:6487634). Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites (By similarity). Acts as a neurotrophic factor that promotes astrocytosis and axonal proliferation (By similarity). Involved in innervation of thermogenic adipose tissue by acting as an adipocyte-derived neurotrophic factor that promotes sympathetic innervation of adipose tissue (By similarity). Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase (By similarity). Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization (PubMed:20351179). May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity (PubMed:22399290). |
| Cellular Location | Cytoplasm. Nucleus. Secreted {ECO:0000250|UniProtKB:P50114} Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114} |
| Tissue Location | Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues |
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Provided below are standard protocols that you may find useful for product applications.
Background
S100B is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21; however, this gene is located at 21q22.3. This protein may function in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.
References
Davila, S., et al. Genes Immun. 11(3):232-238(2010) Mori, T., et al. Glia 58(3):300-314(2010) Steiner, J., et al. Psychoneuroendocrinology 35(2):321-324(2010)
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