Name :
Recombinant Human S100A6 Protein (His Tag), HPLC-verified

Biological Activity :

Background :
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. S100A6 (S100 calcium-binding protein A6) is a member of the S100 family of proteins, and functions in prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of S100A6 have been implicated in melanoma.

Biological Activity :
Testing in progress

Expression Host :
Human

Source :
Baculovirus-Insect Cells

Tag :

Protein Accession No. :
NP_055439.1

NCBI Gene ID :

Synonyms :

Synonyms :
S100 calcium binding protein A6

Amino Acid Sequence :

Molecular Weight :
The recombinant human S100A6 consisting of 101 amino acids and migrates as an approximately 12 kDa band in SDS-PAGE under reducing conditions as predicted.

Purity :
≥ 96 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC.

State of Matter :

Product Concentration :

Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method

Protein Construction :
A DNA sequence encoding the human S100A6 (NP_055439.1) (Met 1-Gly 90) was expressed, with a C-terminal polyhistidine tag.

Buffer Solution :
Lyophilized from sterile 50mM Tris, 100mM NaCl, 0.5mM PMSF, 1mM TCEP, pH 8.0Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :
2A9 Protein, Human; 5B10 Protein, Human; CABP Protein, Human; CACY Protein, Human; PRA Protein, Human S100A6 背景信息 S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. S100A6 (S100 calcium-binding protein A6) is a member of the S100 family of proteins, and functions in prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of S100A6 have been implicated in melanoma.

References & Citations :
Schäfer, B.W. et al., 1996, Trends Biochem. Sci. 21 (4): 134-140. Donato,R. et al., 2003, Microsc. Res. Tech. 60 (6): 540-551. Nowotny, M. et al., 2003, J. Biol. Chem. 278 (29): 26923-26928. Nonaka D, et al., 2008, J. Cutan. Pathol. 35 (11): 1014-1019. Marenholz, I. et al., 2004, Biochem. Biophys. Res. Commun. 322 (4): 1111-22.

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