|Application ||WB, IHC|
|Calculated MW||11203 Da|
|Other Names||Protein S100-A10, Calpactin I light chain, Calpactin-1 light chain, Cellular ligand of annexin II, S100 calcium-binding protein A10, p10 protein, p11, S100A10, ANX2LG, CAL1L, CLP11|
|Target/Specificity||A synthetic peptide corresponding to residues in human Calpactin I light chain/S100A10 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Calpactin-I Antibody (light chain) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ANX2LG, CAL1L, CLP11|
|Function||Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine- specific kinase.|
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Provided below are standard protocols that you may find useful for product applications.
S100 proteins are low-molecular-weight calcium-binding proteins of the EF-hand superfamily and appear to be involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation (1). The Calpactin I light chain (S100 calcium-binding protein A10; S100A10) is a member of the S100 family and it forms a heterotetrameric complex with another calcium-binding protein, annexin II(2). S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane (3). The basic unit for S100A10 is a tight, non-covalent dimmer (4). S100A10, as well as a few other members of the S100 family, are suggested as transglutaminase substrates. Also, S100 proteins have been reported to localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events (3).
1. Schafer BW, et al. Genomics 25(3):638-43, 1995
2. Kube E, et al. Gene. 102(2):255-9, 1991
3. Broome AM, et al. J Histochem Cytochem 51(5):675-685, 2003
4. Rety S, et al. Nat Struct Biol. 6(1):89-95, 1999
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