Anti-SSH2 (full length) polyclonal antibody

Subliminal channels, discovered by Simmons, yield a possibility to transmit covert messages by embedding them in cryptographic digital data, such as (EC)DSA signatures. The embedded messages are used for transmitting important information, or as watermarks or imprints of the data. Anyone can use or abuse these channels very easily because most cryptographic digital data widely used in the Internet is not subliminal-free. For example, DSA signatures are not subliminal-free and they are widely used in various applications, such as PGP, SSH2 and so on. It is very important to evaluate the ability of such channels. In this paper, we evaluate the channel capacity of narrow-band subliminal channels where a transmitter tries only the limited number of input values. Then, we apply this result to a practical model where carriers are transmitted one after another successively. (A carrier denotes data in which a covert message is embedded.) We show, under this model, memories can be used to increase the channel capacity, and then we compare their channel capacities. In addition, we show it is possible to reduce the computational complexity of establishing a narrow-band subliminal channel.

Recently, "superbinder" SH2 domain variants with three amino acid substitutions (sSH2) were reported to have 100-fold or greater affinity for protein-phosphotyrosine (pY) than natural SH2 domains. Here we report a protocol in which His-tagged Src sSH2 efficiently captures pY-peptides from protease-digested HeLa cell total protein extracts. Affinity purification of pYpeptides by this method shows little bias for pY-proximal amino acid sequences, comparable to that achieved by using antibodies to pY, but with equal or higher yield. Superbinder-SH2 affinity purification mass spectrometry (sSH2-AP-MS) therefore provides an efficient and economical approach for unbiased pY-directed phospho-proteome profiling without the use of antibodies.