The streptavidin molecule consists of four identical peptide chains, and the contents of glycine and alanine are relatively large in the amino acid composition, and the active group binding biotin is also the tryptophan residue in the peptide chain. Streptavidin is a slightly acidic (pH6.0) protein and does not carry any sugar groups. Under the action of proteolytic enzyme, streptavidin can be broken between N-terminal 10 ~ 12 and C-terminal 19 ~ 21, and the formed core streptavidin still maintains the complete ability to bind biotin. The activity unit of streptavidin is also expressed in terms of the amount required to bind 1μg biotin, and the high activity of 1mg streptavidin can reach 18U.
streptavidin (SA) is a protein secreted by streptomyces avidinii with a molecular weight of 65kD. Streptavidin molecules are composed of four identical peptide chains, each of which can bind a biotin without any sugar group, so like avidin, one streptavidin molecule can also bind four biotin molecules, and the affinity constant (K) of both is 1015mol/L. Streptavidin is more widely applicable than avidin.
Cat.No
DC66164
Name
DSPE-PEG-Streptavidin
Chemical Properties
CAS
Formula
MW
Storage
2 years -20°C Powder, 2 weeks 4°C in DMSO, 6 months -80°C in DMSO
References
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