Recombinant Mouse S100B Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-4141

Recombinant Mouse S100B Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-4141
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Product Overview

Tag Fc
Host Species Mouse
Accession P50114
Synonym AI850290, Bpb
Background S1B is a member of the S1 family of proteins containing two EF-hand-type calcium-binding motifs. S1B exerts both intracellular and extracellular functions. Intracellular S1B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S1B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes (i.e. beneficial or detrimental, pro-proliferative or pro-differentiative) depending on the concentration attained by the protein, the cell type and the microenvironment. This calcium binding astrocyte-specific cytokine, presents a marker of astrocytic activation and reflects CNS injury. The excellent sensitivity of S1B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. Recent findings provide evidence, that S1B may decrease neuronal injury and/or contribute to repair following traumatic brain injury (TBI). Hence, S1B, far from being a negative determinant of outcome, as suggested previously in the human TBI and ischemia literature, is of potential therapeutic value that could improve outcome in patients who sustain various forms of acute brain damage.
Description A DNA sequence encoding the mouse S100B (P50114) (Ser2-Glu92) was expressed with the fused Fc region of human IgG1 at the N-terminus.
Source HEK293
Predicted N Terminal Glu
AA Sequence Ser2-Glu92
Molecular Weight The recombinant mouse S100B/Fc comprises 351 a.a. and has a predicted molecular mass of 39 kDa. The apparent molecular mass of the protein is approximately 41 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity >80% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. Measured by its binding ability in a functional ELISA.2. Immobilized recombinant mouse S100B-Fc at 10 ug/ml (100 ul/well) can bind biotinylated recombinant human AGER with a linear range of 0.03-0.5 ug/ml.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Subcellular Location Cytoplasm. Nucleus.
Protein Families S-100 family
Database References
Tissue Specificity Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.

Gene Functions References

  1. Data (including data from studies in knockout mice) suggest that S100b acting as a humoral factor impairs glycolysis in muscle (myoblasts, myotubes, and skeletal muscles) independent of insulin action; this effect appears to be due to inhibition of Gapdh activity from enhanced poly(ADP-ribosyl)ation of Gapdh. (S100B = S100 protein, beta polypeptide, neural; Gapdh = glyceraldehyde-3-phosphate dehydrogenase) PMID: 28174179
  2. S100B inhibits C3H/10T1/2 murine embryonic mesenchyma.l cells into osteoblasts. S100B stimulates C3H/10T1/2 cell differentiation into adipocytes. PMID: 27601207
  3. The results of this study showed that S100B affects behavioral despair in female mice through functional interaction with the 5-HT7 receptor. PMID: 26499172
  4. Data show that S100B has direct effects on macrophages, enhancing particularly CCL22 and IL-1beta expression and modulates the inflammatory response in uveoretinitis and this is likely to be, at least in part, via a direct effect on macrophages. PMID: 26204512
  5. Data show that high glucose increased protein-protein interaction between Steap4 and S100B in mesangial (MES13) cells. PMID: 25817898
  6. high glucoseinduced profibrotic genes (TGFbeta, type IV collagen and fibronectin) and cell hypertrophyrelated p21WAF1 are dependent on S100B. PMID: 25482070
  7. Data suggest up-regulation of S100b/RAGE (advanced glycosylation end-product receptor) signaling plays role in inflammatory interaction between adipocytes/macrophages; adipocyte secretion of S100b is up-regulated by Tnf (tumor necrosis factor-alpha). PMID: 23804363
  8. Gioma production of S100B enhancestumor growth through CCL2 upregulation and tumor-associated macrophages chemoattraction. PMID: 23719262
  9. HMGB1, S100B, and RAGE signaling modulate the hippocampal inflammatory response and might play key roles in surgery-induced cognitive decline. PMID: 23899512
  10. S100B is a proinflammatory cytokine bridging RAGE and CD166/ALCAM downstream effector mechanisms, both being compensatory upregulated after genetic deletion of its counterpart. PMID: 23729438
  11. S100B expression may serve to modulate cardiac metabolism and adverse consequences of AGE in diabetic post-MI remodeling and function PMID: 23000886
  12. S100B is expressed in mouse photoreceptor cone outer segments but not in rods. PMID: 22508049
  13. The RAGE pathway may play an important role in STAT3 induction in glioma-associated macrophages and microglia, a process that may be mediated through S100B. PMID: 21264954
  14. S100B and APP levels are simultaneously increased within Down syndrome neural progenitors, their secretions are synergistically enhanced in a paracrine fashion, and their overexpressions disrupt mitochondrial membrane potentials and redox states. PMID: 21779383
  15. Unlike in the hippocampus-dependent tasks, S100B-KO mice were indistinguishable from wild-type mice in both cerebellum-dependent motor coordination and delay eyeblink conditioning. PMID: 21146588
  16. Data support S100B inhibition as a novel strategy for reducing cortical plaque load, gliosis and neuronal dysfunction in Alzheimer disease (AD) and suggest that both extracellular as well as intracellular S100B contribute to AD histopathology. PMID: 21080947
  17. These results suggest that S100beta is important for brain development and establishment of proper brain functions. PMID: 20099023
  18. Given the crucial roles of COX-2, IL-1beta and TNF-alpha in the inflammatory response, we propose that, by engaging RAGE, S100B might play an important role in microglia activation in the course of brain damage. PMID: 18599158
  19. attenuates the hemodynamic response to catecholamines PMID: 19713945
  20. constitutive overexpression of S100beta in transgenic mice does not modify serotonin levels during development, nor does it protect the serotonergic neurons from selective neurotoxicity or modify the serotonergic sprouting induced by partial lesion. PMID: 11835317
  21. The distribution of serotonergic fibers in the brains of S100B-knockout mice was normal. S100B may not influence neurite extension of serotonergic neurons PMID: 11872254
  22. Glial protein S100B modulates long-term neuronal synaptic plasticity PMID: 11891290
  23. the major cytoplasmic S100B target protein in different glial cell lines in the presence of Zn(2+) and Ca(2+) is IQGAP1 PMID: 12377780
  24. These results implicate normal levels of S100B in the attenuation of epileptogenesis. PMID: 12393261
  25. the -1,669/+3,106 sequence of the S100B gene is a useful reagent for driving expression of transgenes in most S100B-expressing cells of mouse brain. PMID: 12561079
  26. S-100b-containing cells and GFAP-containing cells increased in the striatum and substantia nigra at 3 days after MPTP treatment. S-100 immunoreactivity was observed only in GFAP-positive astrocytes. PMID: 12673835
  27. S-100 beta overexpressing animals were more active than the CD-1 control animals and showed significantly less social sniffing. PMID: 12742260
  28. Our findings show increased clusterin expression in the aged S100B mice compared to their CD-1 controls, a finding we have interpreted as further evidence of pathological brain aging. PMID: 15126113
  29. results support the idea that elevated levels of S100B in the brain are associated with increased vulnerability to neurological injury PMID: 15236402
  30. Mice lacking S100B show an apparent delay in OPC maturation in response to demyelinating insult. Nuclear S100B participates in the regulation of oligodendroglial cell maturation. PMID: 15555923
  31. 5-HT may modulate glial morphology by inducing a release of intracellular S-100B, and this pathway is inoperable in the S-100B knockout (-/-). PMID: 15621007
  32. These results argue against the current view that S100B expression is restricted to the astrocytic lineage in the CNS, and indicate that the use of S100B in combination with other molecular markers will help discriminate oligodendrocytes from astrocytes. PMID: 15782413
  33. Our data are consistent with a model in which S-100B overexpression in AD enhances glial activation and leads to an augmented neuroinflammatory process that increases the severity of neuropathologic sequelae. PMID: 15810011
  34. Altogether, our results indicate that the S100B expression defines a late developmental stage after which GFAP-expressing cells lose their NSC potential and suggest that S100B expression is repressed by adult SVZ microenvironment. PMID: 17078026
  35. possible interaction between FGF-2 and S100Beta in activated satellite cells of the dorsal root ganglia, which might trigger paracrine actions in the axotomized sensory neurons PMID: 17729158
  36. S100B has a role in exacerbating brain damage and periinfarct reactive gliosis (astrocytosis and microgliosis) during the subacute phase of middle cerebral artery occlusion PMID: 18451356
  37. There was a significant increase of hippocampal BDNF (+53%) and a decrease of hippocampal (-12%) and residual neocortical (-15%) NA in 10-month-old S100B KO mice compared to wildtype mice. PMID: 18638525
  38. Our findings suggest further investigation into the potential role of vitamin E in reducing the oxidation state of the S100B protein and its influence on neuroinflammatory processes marked by microglial activation in vivo. PMID: 18649404
  39. The data of this study indicated that genetic differences in S100B gene expression may predispose individual differences in the responsivity to repeated intake of MDMA. PMID: 18812013


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

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