Recombinant Mouse S100 beta Protein

Name: Recombinant Mouse S100 beta Protein
Brand: Beta LifeScience
SKU: BLA-8825P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Mouse
Accession	P50114
Synonym	NEF Protein S100 B Protein S100-B S 100 calcium binding protein beta chain S 100 protein beta chain S-100 protein beta chain S-100 protein subunit beta S100 S100 calcium binding protein beta (neural) S100 calcium-binding protein B S100 protein beta chain S100B S100B_HUMAN S100beta
Description	Recombinant Mouse S100 beta Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKE QEVVDKVMETLDEDGDGECDFQEFMAFVAMVTTACHEFFEHE
Molecular Weight	11 kDa
Purity	>95% purity as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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	KEGG: mmu:20203 STRING: 10090.ENSMUSP00000047968 UniGene: Mm.235998
Tissue Specificity	Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.

Gene Functions References

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
S100B inhibits C3H/10T1/2 murine embryonic mesenchyma.l cells into osteoblasts. S100B stimulates C3H/10T1/2 cell differentiation into adipocytes. PMID: 27601207
The results of this study showed that S100B affects behavioral despair in female mice through functional interaction with the 5-HT7 receptor. PMID: 26499172
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
Data show that high glucose increased protein-protein interaction between Steap4 and S100B in mesangial (MES13) cells. PMID: 25817898
high glucoseinduced profibrotic genes (TGFbeta, type IV collagen and fibronectin) and cell hypertrophyrelated p21WAF1 are dependent on S100B. PMID: 25482070
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
Gioma production of S100B enhancestumor growth through CCL2 upregulation and tumor-associated macrophages chemoattraction. PMID: 23719262
HMGB1, S100B, and RAGE signaling modulate the hippocampal inflammatory response and might play key roles in surgery-induced cognitive decline. PMID: 23899512
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
S100B expression may serve to modulate cardiac metabolism and adverse consequences of AGE in diabetic post-MI remodeling and function PMID: 23000886
S100B is expressed in mouse photoreceptor cone outer segments but not in rods. PMID: 22508049
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
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
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
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
These results suggest that S100beta is important for brain development and establishment of proper brain functions. PMID: 20099023
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
attenuates the hemodynamic response to catecholamines PMID: 19713945
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
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
Glial protein S100B modulates long-term neuronal synaptic plasticity PMID: 11891290
the major cytoplasmic S100B target protein in different glial cell lines in the presence of Zn(2+) and Ca(2+) is IQGAP1 PMID: 12377780
These results implicate normal levels of S100B in the attenuation of epileptogenesis. PMID: 12393261
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
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
S-100 beta overexpressing animals were more active than the CD-1 control animals and showed significantly less social sniffing. PMID: 12742260
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
results support the idea that elevated levels of S100B in the brain are associated with increased vulnerability to neurological injury PMID: 15236402
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
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
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
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
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
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
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
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
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
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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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.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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