Name :
Recombinant Human S100A14 Protein (His Tag)
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 theneural 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. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_065723.1
NCBI Gene ID :
Synonyms :
Synonyms :
S100 calcium binding protein A14
Amino Acid Sequence :
Molecular Weight :
The recombinant human S100A14 consisting of 114 amino acids and migrates as an 13 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity :
> 85 % as determined by SDS-PAGE
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 :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the native human S100A14 (NP_065723.1) (Gly 2-His 104) was expressed, with a polyhistide tag at the N-terminus.
Buffer Solution :
Supplied as sterile 50mM Tris, 20% glycerol, pH 7.5Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
BCMP84 Protein, Human; S100A15 Protein, Human S100A14 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 theneural 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. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.
References & Citations :
Pietas A., et al., 2002, Genomics 79: 513-22. Donato, R. et al., 2003, Microsc. Res. Tech. 60 (6): 540-51. Gebhardt, C. et al., 2006, Biochem Pharmacol. 72 (11):1622-31. Nonaka, D. et al., 2008, J. Cutan. Pathol. 35 (11): 1014-9. Lim, SY. et al., 2008, J Immunol. 181 (8): 5627-36. Heibeck T.H. et al., 2009, J. Proteome Res. 8:3852-61.
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