Name :
Recombinant Human S100A3 Protein (His & MBP Tag)
Biological Activity :
Background :
Protein S100-A3, also known as Protein S-100E, S100 calcium-binding protein A3, S100A3 and S100E, is a member of the S-100 family. S100A3 / S100E contains 2 EF-hand domains. S100A3 / S100E is highly expressed in the differentiating cuticular cells within the hair follicle and organized into mature hair cuticles. High concentrations of S100A3 homotetramer might provide the millimolar level of Ca2+ required for hair cuticular barrier formation. S100A3 / S100E is a unique member of the Ca2+-binding S100 protein family with the highest cysteine content and affinity for Zn2+. S100A3 / S100E binds both calcium and zinc. S100A3 / S100E probably binds 2 zinc ions per molecule. It may be involved in calcium-dependent cuticle cell differentiation and hair shaft formation. S100A3 plays an important role in calcium-dependent processes leading to hair shaft formation. S100A3 / S100E is a unique protein among all members of the calcium-binding S100 family, is specifically expressed at the inner endocuticle of human hair fibers. Upon hair damage, S100A3 / S100E is released from hair fibers and possibly destabilizes the hair tissue architecture.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
P33764
NCBI Gene ID :
Synonyms :
Synonyms :
S100 calcium binding protein A3
Amino Acid Sequence :
Molecular Weight :
The recombinant human S100A3/MBP fusion protein consists of 498 amino acids and has a calculated molecular mass of 55.3 kDa. It migrates as an approximately 50 kDa band in SDS-PAGE under reducing conditions.
Purity :
> 95 % 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 human S100A3 (P33764) (Met 1-Gln 101) was fused with an N-terminal polyhistidine-tagged MBP tag at the N-terminus.
Buffer Solution :
Supplied as sterile PBS, 20% glycerol, pH 7.4Please 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 :
S100E Protein, Human S100A3 背景信息 Protein S100-A3, also known as Protein S-100E, S100 calcium-binding protein A3, S100A3 and S100E, is a member of the S-100 family. S100A3 / S100E contains 2 EF-hand domains. S100A3 / S100E is highly expressed in the differentiating cuticular cells within the hair follicle and organized into mature hair cuticles. High concentrations of S100A3 homotetramer might provide the millimolar level of Ca2+ required for hair cuticular barrier formation. S100A3 / S100E is a unique member of the Ca2+-binding S100 protein family with the highest cysteine content and affinity for Zn2+. S100A3 / S100E binds both calcium and zinc. S100A3 / S100E probably binds 2 zinc ions per molecule. It may be involved in calcium-dependent cuticle cell differentiation and hair shaft formation. S100A3 plays an important role in calcium-dependent processes leading to hair shaft formation. S100A3 / S100E is a unique protein among all members of the calcium-binding S100 family, is specifically expressed at the inner endocuticle of human hair fibers. Upon hair damage, S100A3 / S100E is released from hair fibers and possibly destabilizes the hair tissue architecture.
References & Citations :
Kizawa, K. et al., 2008, J Biol Chem. 283 (8):5004-13. Kizawa, K. et al., 1998, J Invest Dermatol. 111 (5):879-86. Kizawa, K. et al., 2002, Biochem Biophys Res Commun. 299 (5):857-62. Fritz,G. et al., 2002, J Biol Chem. 277 (36):33092-8.
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