Recombinant Mouse S100A4 Protein, CF

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Recombinant Mouse S100A4 Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Measured by its ability to enhance neurite outgrowth of dissociated E13 chick embryonic dorsal root ganglia (DRG) neurons. Recombinant mouse S100A4 is able to significantly enhance neurite outgrowth when immobilized as a 3 µL droplet containing 90 ng on a nitrocellulose-coated microplate.
E. coli-derived mouse S100A4 protein
Ala2-Lys101, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
12.4 kDa

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS and DTT.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: S100A4

S100A4 (also named metastasin, Mtsl and calvasculin) is an 11 kDa member of the S100 (soluble in 100% saturated ammonium sulfate) family of proteins (1 - 5). The S100 family is a further classified as a member of the EF-hand superfamily of Ca++-binding proteins. These participate in both calcium-dependent and calcium-independent protein-protein interactions. The hallmark of this superfamily is the EF-hand motif that consists of a Ca++-binding site flanked by two alpha -helices (helix E and helix F) that were originally identified in a right-handed model of carp muscle calcium-binding protein (6). Mouse S100A4 is 101 amino acids (aa) in length (1, 2). It contains two EF hand domains, one between aa 12 - 47, and a second between aa 50 - 85. The first domain has a 14 aa cation-binding motif and binds Ca++ with low affinity. The second Ca++-binding motif is 12 aa in length and binds Ca++ with high affinity. S100A4 has no classical signal sequence but is secreted from cells (3, 7). Mouse S100A4 shares 93%, 96% and 89% aa identity with human, rat and canine S100A4, respectively. S100A4 exists as dimer (8, 9, 10). Extracellular S100A4 is reported to induce MMP production, activate MMPs, promote neurite outgrowth and stimulate cardiomyocyte proliferation (4, 10, 11, 12, 13). Within the cell, dimers are likely the functional unit. Here, they are constitutive homo- or heterodimers (with S100A1) that interact with Ca++, undergo a conformational change, and subsequently bind to cytoplasmic targets. Known targets include p53, myosin heavy chain II, F-actin and liprin beta 1 (4, 14). In general, it can be said that S100A4 blocks target phosphorylation and multimerization (4, 7, 14). S100A4 activity has been associated with cell transformation. It seems likely this is either coincidental, or a consequence, rather than a cause of transformation (3).

  1. Jackson-Grusby, L.L. et al. (1987) Nucleic Acids Res. 15:6677.
  2. Goto, K. et al. (1988) J. Biochem. 103:48.
  3. Garrett, S.C. et al. (2006) J. Biol. Chem. 281:677.
  4. Santamaria-Kisiel, L. et al. (2006) Biochem. J. 396:201.
  5. Donato, R. (2001) Int. J. Biochem. Mol. Biol. 33:637.
  6. Kretsinger, R.H. and C.E. Nockolds (1973) J. Biol. Chem. 248:3313.
  7. Helfman, D.M. et al. (2005) Br. J. Cancer 92:1955.
  8. Burkitt, W.I. et al. (2003) Biochem. Soc. Trans. 31:985.
  9. Vallaly, K.M. et al. (2002) Biochemistry 41:12670.
  10. Novitskaya, V. et al. (2000) J. Biol. Chem. 275:41278.
  11. Stary, M. et al. (2006) Biochem. Biophys. Res. Commun. 343:555.
  12. Semov, A. et al. (2005) J. Biol. Chem. 280:20833.
  13. Saleem, M. et al. (2006) Proc. Natl. Acad. Sci. USA 103:14825.
  14. Kriajevska, M. et al. (2002) J. Biol. Chem. 277:5229.
Long Name
S100 Calcium Binding Protein A4
Entrez Gene IDs
6275 (Human); 20198 (Mouse); 24615 (Rat)
Alternate Names
18A2; 42A; Calvasculin; CAPL; CAPLS100 calcium binding protein A4 (calcium protein, calvasculin, metastasin; fibroblast-specific protein-1,42A; FSP1; leukemia multidrug resistance associated protein; malignant transformation suppression 1; Metastasin; MTS1; murine placental homolog); P9KA; PEL98; Placental calcium-binding protein; Protein Mts1; protein S100-A4; S100 calcium binding protein A4; S100 calcium-binding protein A4 (calcium protein, calvasculin, metastasin, murine placental homolog); S100 calcium-binding protein A4; S100A4

Citation for Recombinant Mouse S100A4 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Identification of a pro-angiogenic functional role for FSP1-positive fibroblast subtype in wound healing
    Authors: S Saraswati, SMW Marrow, LA Watch, PP Young
    Nat Commun, 2019;10(1):3027.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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