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Recombinant Human S100A4 Protein (His Tag)

Uniprot : P26447
  • Cat.No.:PKSH033548

  • Expression host: E.coli

To Purchase PKSH033548

Size:
  • 10μg
  • 50μg
Price: $92
Qty:

Description

Synonyms Protein S100-A4;Calvasculin;Metastasin;Placental calcium-binding protein;Protein Mts1;S100 calcium-binding protein A4;S100A4;CAPL;MTS1;18A2;42A;FSP1;P9KA;PEL98
Species Human
Expression_host E.coli
Sequence Met1-Lys101
Accession P26447
Mol_Mass 12.6 kDa
AP_Mol_Mass 13 kDa
Tag C-His

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin level < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 6% Sucrose, 4% Mannitol, 50mM NaCl, 0.05% Tween 80, pH 7.0.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specif
Reconstitution Please refer to the printed manual for detailed information.

Background

S100A4 is a member of the S100 family of proteins. The S100 family is 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 α-helices (helix E and helix F) that were originally identified in a right-handed model of carp muscle calcium-binding protein. Human S100A4 is 101 amino acids (aa) in length. It contains two EF hand domains, one between aa 12-47, and a second between aa 50-85. S100A4 activity has been associated with cell transformation. It seems likely this is either coincidental, or a consequence, rather than a cause of transformation.

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