Anti-S100B Antibody Trial Size

Cell Markers, Glial and Schwann Cell Markers, Astrocyte Markers

United States

14 kDa

Phosphate-buffered (10 mM) isotonic (0.9%, w/v) saline (“PBS, " pH 7.2) with sodium azide (0.02%, w/v) added as a preservative.

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 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.

Polyclonal

1:500-1:1000

His tagged full length protein

No cross-reactivity reported

Affinity-Purified IgY

Yes

Eggs from hens hyperimmunized with target were used to prepare an IgY fraction which was then subjected to antigen-specific affinity purification.