Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

S100A10 (4E7E10) Mouse mAb #5529

Applications Reactivity Sensitivity MW (kDa) Isotype
W IHC-P IF-IC F H Mk Endogenous 11 Mouse IgG1

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

S100A10 (4E7E10) Mouse mAb recognizes endogenous levels of total S100A10 protein. This antibody is not known to react with other S100 family proteins.

Source / Purification

Monoclonal antibody is generated by immunizing animals with a recombinant fragment of human S100A10 protein expressed in E. coli. The antibody is affinity purified by Protein G chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using S100A10 (4E7E10) Mouse mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human prostate using S100A10 (4E7E10) Mouse mAb.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of Jurkat cells (blue) and HEK001 cells (green) using S100A10 (4E7E10) Mouse mAb.


IF-IC

IF-IC

Confocal immunofluorescent analysis of HEK001 cells using S100A10 (4E7E10) Mouse mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

Background

Despite their relatively small size (8-12 kDa) and uncomplicated architecture, S100 proteins regulate a variety of cellular processes such as cell growth and motility, cell cycle progression, transcription, and differentiation. To date, 25 members have been identified, including S100A1-S100A18, trichohyalin, filaggrin, repetin, S100P, and S100Z, making it the largest group in the EF-hand, calcium-binding protein family. Interestingly, 14 S100 genes are clustered on human chromosome 1q21, a region of genomic instability. Research studies have demonstrated that significant correlation exists between aberrant S100 protein expression and cancer progression. S100 proteins primarily mediate immune responses in various tissue types but are also involved in neuronal development (1-4).Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cation in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4).

S100A10 (alternately known as p11 or calpactin 1 light chain) forms a constitutive heterotetramer with annexin-A2 (ANXA2) and may act as a bridge between the plasma membrane and actin cytoskeleton via interactions with the plasma membrane (via ANXA2) and various protein partners such as the SNARE complex or actin (5-7). S100A10 has been hypothesized to play a critical role in neuronal signaling due to its interaction and regulation of neurotransmitter receptors and neuron-specific ion channels such as 5-HT1B, TRPV5, ASIC1, TASK1 and NaV1.8 (8-10). More recently, S100A10 has also been shown to modulate macrophage activation and invasion via its ability to bind and transmit receptor-like signals in response to plasminogen (11,12).

  1. Heizmann, C.W. et al. (2002) Front Biosci 7, d1356-68.
  2. Donato, R. (2003) Microsc Res Tech 60, 540-51.
  3. Marenholz, I. et al. (2004) Biochem Biophys Res Commun 322, 1111-22.
  4. Santamaria-Kisiel, L. et al. (2006) Biochem J 396, 201-14.
  5. Illien, F. et al. (2010) Biochim Biophys Acta 1798, 1790-6.
  6. Umbrecht-Jenck, E. et al. (2010) Traffic 11, 958-71.
  7. Jung, M.J. et al. (2010) Exp Cell Res 316, 1234-40.
  8. van de Graaf, S.F. et al. (2003) EMBO J 22, 1478-87.
  9. Girard, C. et al. (2002) EMBO J 21, 4439-48.
  10. Donier, E. et al. (2005) J Biol Chem 280, 38666-72.
  11. O'Connell, P.A. et al. (2010) Blood 116, 1136-46.
  12. Swisher, J.F. et al. (2010) Blood 115, 549-58.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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