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This paper demonstrates wide-band CMOS VCO based on the transformer feedback from traditional circuit to our proposed work. The start up condition of the traditional cross-coupled pair is expressed by the high frequency model. The wide band technique of this structure is derived with the help of the high frequency model of the transistor. Therefore, the wide band CMOS VCO based on the common source transformer feedback topology can achieves the high performance in the low voltage and low phase noise. The measurement result of the VCO exhibits the figure of merit, core power consumption and output power at supply voltage 0.8 V are –193.1 dBc/Hz, 4.4 mW and –2.3 dBm, respectively. The phase noise is –124.3 dBc/Hz at 1 MHz offset under the operation frequency 5.8 GHz. And the tuning range of the circuit can obtain 28%, this VCO is fabricated in TSMC 0.18 μm 1P6MCMOS process.
RP215 is one of the three thousand monoclonal antibodies
(Mabs) which were generated against the OC-3-VGH ovarian cancer cell line.
RP215 was shown to react with a carbohydrate-associated epitope located
specifically on glycoproteins, known as CA215, from cancer cells. Further
molecular analysis by matrix
adsorption laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) revealed that CA215 consists mainly of immunoglobulin super-family
(IgSF) proteins, including immunoglobulins, T-cell receptors, and cell
adhesion molecules, as well as several other unrelated proteins. Peptide
mappings and glycoanalysis were performed with CA215 and revealed high-mannose
and complex bisecting structures with terminal sialic acid in N-glycans. As
many as ten O-glycans, which are structurally similar to those of mucins, were
also identified. In addition, two additional O-linked glycans were exclusively
detected in cancerous immunoglobulins but not in normal B cell-derived immunoglobulins.
Immunizations of mice with purified CA215 resulted in the predominant
generation of RP215-related Mabs, indicating the immunodominance of this
carbohydrate-associated epitope. Anti-idiotype (anti-id) Mabs of RP215, which
were generated in the rat, were shown to contain the internal images of the
carbohydrate-associated epitope. Following immunizations of these anti-id
Mabs in mice, the resulting anti-anti-id (Ab3) responses in mice were found to be immunologically similar to
that of RP215. Judging from these observations, anti-id Mabs, which
carry the internal image of the RP215-specific epitope, may be suitable
candidates for anticancer vaccine development in humans.