Form
Liquid
Buffer
0.02M Potassium Phosphate, 0.15M NaCl
Preservative
0.01% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
5 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Bovine
Immunogen
This Protein A purified antibody was prepared from whole rabbit serum produced by repeated immunizations with full-length bovine S100 protein (mixture of aa homodimers and ab heterodimers).
Purification
Protein A purified
Conjugation
Unconjugated
RRID
AB_11179831
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
protein S100-A1
Background
S-100 protein derived from brain tissue is an acidic calcium-binding protein with molecular weight of about 21kDa. In human brain tissue S-100 protein is mainly presented as two isoforms - bb homodimer (S-100b) and ab heterodimer (S-100a). Because of its predominant location in astroglial cells S-100 protein can be used as a sensitive and reliable marker for central nervous system injury. Structural damage of glial cells causes leakage of S-100 protein into the extracellular matrix and into cerebrospinal fluid, further releasing into the bloodstream. Measurements of S-100 protein in patient serum samples are useful in monitoring of traumatic brain injury, ischemic brain damage after circulatory arrests, and in diagnosis and prognosis of clinical outcome in acute stroke. Although predominant among the water-soluble brain proteins, S-100 is also found in a variety of other tissues. S-100 is an intracellular protein that weakly binds calcium. It binds zinc very tightly, however, and this appears to increase the affinity of the protein for calcium. 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.
Database
Research Area