Anti-S100B Antibody

S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis.

Our Anti-S100B chicken polyclonal primary antibody from Aves Labs is produced in-house. It detects human, mouse, and rat S100B, and is affinity-purified igy. It is great for use in ICC, WB.

S100 Calcium Binding Protein B, S100beta, S-100 Protein Subunit Beta, Protein S100-B, S100 Calcium Binding Protein, Beta (Neural), S100 Calcium-Binding Protein B, S-100 Protein Beta Chain, S100-B, S100, NEF

Store at 4°C in the dark. Under these conditions, the antibodies should have a shelf life of at least twelve months, provided they remain sterile. For longer term storage, aliquot and freeze to avoid freeze-thaw of the antibody.

S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis. S100 protein is a type of low molecular weight protein found in vertebrates characterized by two calcium binding sites of the helix-loop-helix ("EF-hand type") conformation. There are at least 21 different types of S100 proteins. The name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are homodimeric, consisting of two identical polypeptides held together by non-covalent bonds. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. Although S100 proteins are structurally similar to calmodulin, they differ in that they are cell-specific, expressed in particular cells at different levels depending on environmental factors. By contrast, calmodulin is a ubiquitous and universal intracellular Ca++ receptor widely expressed in many cells. S-100 is normally present in cells derived from the neural crest (Schwann cells, melanocytes, and glia cells), chondrocyte, adipocytes, myoepithelial cells, macrophages, Langerhans cells, dendritic cells, and keratinocytes. It may be present in some breast epithelial cells. This antibody stains schwannoma, ependymomas, astrogliomas, almost all benign and malignant melanoma and their metastasis.

Each new lot of this antibody is tested to confirm that it recognizes a single immunoreactive band of expected molecular weight when used to probe brain lysate.