<result><Target><Item><Target_ID> 1</Target_ID>
<Target_Name>Anti-Ogawa O-antigen monoclonal antibody S-20-4</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>GI:9954938, GI:9954939</Target_Sequence>
<Synonyms>Mab S-20-4</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure>1F4W, 1F4X, 1F4Y</Target_Structure>
<Comments>S-20-4 mAb is an IgG1 specific for Ogawa O-antigen (O-specific polysaccharide; O-SP) of V. cholerae O1. Among solved structures, 1F4W contains the unliganded Fab fragment; 1F4X is the Fab fragment complexed with MGS; 1F4Y is the Fab fragment complexed with MGU.</Comments>
</Item><Item><Target_ID> 2</Target_ID>
<Target_Name>Anti-IA-2 monoclonal antibody 96/3</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>H Chain : QVQLQESGPGLVKPSETLSLRCNVSGVSISGFYWGWIRQPPGKGLEWIGHIFSSGSTDYSPSLKSRVDVSMDTSKNHFSLKLSSVTAADTAVYYCARVLKGVATASFDFWGRGTLVTVSS
L Chain: SYVLTQPPSVSVAPGKTATITCGADNIGTKSVHWYQQRPGQAPMLVIYYNKNRPSGIPERFSGSNSGHTATLTISRVEAGDEAAYYCQVWDTRSDLVVFGGGTKLTVLG</Target_Sequence>
<Synonyms>Mab 96/3</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure></Target_Structure>
<Comments>B lymphocytes from 11 insulin-dependant diabetes mellitus (IDDM) patients exhibiting high anti-IA-2 Ab levels in their sera were subjected to EBV immortalization. Cell line 96/3 from patient 9 (2 years duration of IDDM) is the only cell line showed long term stability for 12 month and could be used as constant source of anti-IA-2 Ab with a production rate of 5-8 mg/million cells in 24 h. Anti-IA-2 monoclonal antibody 96/3 belongs to IgG1 subclass and λ type. And it also revealed high affinity to recombinant IA-2ic (KD=0.13 nM) by the BIAcore method. The nucleotide sequences of hAb96/3 were determined by cloning of the VL and VH DNA fragments as scFv Abs. The  amino acid sequences were then derived. However, the sequences were not included in the GenBank.</Comments>
</Item><Item><Target_ID> 3</Target_ID>
<Target_Name>Anti-AMA1 monoclonal antibody 4G2dc1</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Mab 4G2dc1</Synonyms>
<Target_Source>Rattus norvegicus (Rat):10116</Target_Source>
<Target_Structure></Target_Structure>
<Comments>Rat monoclonal antibody 4G2dc1 recognizes correctly folded AMA1 and blocks merozoite invasion of erythrocytes.</Comments>
</Item><Item><Target_ID> 4</Target_ID>
<Target_Name>C-C chemokine receptor type 5, CCR5</Target_Name>
<Target_Type>Protein&gt;Receptor</Target_Type>
<Target_Sequence>P51681</Target_Sequence>
<Synonyms>CCR-5, CC-CKR-5, C-C CKR-5
HIV-1 fusion coreceptor
CHEMR13
CD_antigen=CD195</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>2L87, 2RLL, 2RRS, 4MBS</Target_Structure>
<Comments>CCR5 is a member of the beta chemokine receptors family of integral membrane proteins. In Humans, the CCR5 gene location is on the short (p) arm at position 21 on chromosome 3. Certain populations have inherited the Delta 32 mutation resulting in the genetic deletion of a portion of the CCR5 gene. Homozygous carriers of this mutation are resistant to M-tropic strains of HIV-1 infection. There are several theoretical structure models of CCR5 in the PDB database, i.e. 1ND8, 1NE0, 1OPN, 1OPT and 1OPW.</Comments>
</Item><Item><Target_ID> 5</Target_ID>
<Target_Name>Interleukin-6 receptor subunit alpha</Target_Name>
<Target_Type>Protein&gt;Receptor</Target_Type>
<Target_Sequence>P08887</Target_Sequence>
<Synonyms>IL-6 receptor subunit alpha, IL-6R subunit alpha, IL-6R-alpha, IL-6RA
IL-6R 1
Membrane glycoprotein 80, gp80
CD_antigen=CD126</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1N26, 1P9M, 2ARW</Target_Structure>
<Comments></Comments>
</Item><Item><Target_ID> 6</Target_ID>
<Target_Name>EWS-Fli1 protein</Target_Name>
<Target_Type>Protein&gt;Others</Target_Type>
<Target_Sequence>Q16198</Target_Sequence>
<Synonyms></Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure></Target_Structure>
<Comments></Comments>
</Item><Item><Target_ID> 7</Target_ID>
<Target_Name>Anti-CD20 monoclonal antibody rituximab</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>GI:146387640, GI:146387641</Target_Sequence>
<Synonyms>IDEC-C2B8
Rituxan
MabThera</Synonyms>
<Target_Source>Homo sapiens (Human):9606, Mus musculus (Mouse):10090</Target_Source>
<Target_Structure>2OSL</Target_Structure>
<Comments>Rituximab is a chimeric IgG1κ antibody against CD20. It was initially developed by IDEC Pharmaceuticals under the name IDEC-C2B8. It was approved by the U.S. Food and Drug Administration in 1997 to treat B-cell non-Hodgkin lymphomas resistant to other chemotherapy regimens. Now it is used in the treatment of many lymphomas, leukemias, transplant rejection and some autoimmune disorders.</Comments>
</Item><Item><Target_ID> 8</Target_ID>
<Target_Name>Anti-CD25 monoclonal antibody basiliximab</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>GI:284793973, GI:284793974, GI:284793975, GI:284793976, GI:284793977, GI:284793978</Target_Sequence>
<Synonyms>Simulect</Synonyms>
<Target_Source>Homo sapiens (Human):9606, Mus musculus (Mouse):10090</Target_Source>
<Target_Structure>3IU3</Target_Structure>
<Comments>Basiliximab (trade name Simulect) is a chimeric (murine/human) monoclonal antibody (IgG1κ) against CD25. It was approved by the Food and Drug Administration in 1998 and used to prevent rejection in organ transplantation, especially in kidney transplants.</Comments>
</Item><Item><Target_ID> 9</Target_ID>
<Target_Name>Baculoviral IAP repeat-containing protein 4</Target_Name>
<Target_Type>Protein&gt;Enzyme</Target_Type>
<Target_Sequence>P98170</Target_Sequence>
<Synonyms>E3 ubiquitin-protein ligase XIAP
Inhibitor of apoptosis protein 3, IAP-3, hIAP-3, hIAP3
X-linked inhibitor of apoptosis protein, X-linked IAP
IAP-like protein, ILP, hILP
EC=6.3.2.-</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1C9Q, 1F9X, 1G3F, 1G73, 1I3O, 1I4O, 1I51, 1KMC, 1NW9, 1TFQ, 1TFT, 2ECG, 2JK7, 2KNA, 2OPY, 2OPZ, 2POI, 2POP, 2QRA, 2VSL, 3CLX, 3CM2, 3CM7, 3EYL, 3G76, 3HL5</Target_Structure>
<Comments>XIAP functions as a caspase inhibitor and is a member of the inhibitors of apoptosis (IAP) family of proteins.</Comments>
</Item><Item><Target_ID> 10</Target_ID>
<Target_Name>Anti-glycoprotein E2 monoclonal antibody AP33</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>GI:406855809, GI:4068558010, GI:4068558011, GI:4068558012, GI:4068558013, GI:4068558014</Target_Sequence>
<Synonyms>Mab AP33</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure>4G6A</Target_Structure>
<Comments>Monoclonal antibody AP33 (MAb AP33) was generated by the following procedure. BALB/c mice were immunized subcutaneously with 20 μg of a recombinant form of mammalian cell-expressed HCV strain Gla E1E2 emulsified in Freund\'s complete adjuvant. After 4 weeks, the animals were boosted with E1E2 emulsified in Freund\'s incomplete adjuvant. Mice were further boosted twice at 2-week intervals. Eight days following the last injection, the sera from tail bleeds were tested for E1E2-specific antibodies. Three weeks following the last boost, the animals were given a final intraperitoneal injection of 100 μg of purified recombinant E1E2. Spleen cells from immunized animals were removed 5 days postinjection and fused with Sp2/0-Ag 14 myeloma cells (ratio, 10:1) by using 50% polyethylene glycol 1500 in DMEM. Cells were then resuspended in HAT medium (EFC10 supplemented with histone acetyltransferase) and 20% conditioned medium (i.e., clarified EFC10 that had previously been used to grow Sp2/0 cells), plated out into 96-well microtiter plates, placed in a CO2 humidified incubator at 37°C, and left for 12 to 14 days. Medium from wells containing colonies was removed and screened by ELISA for E1E2-specific MAbs. Cells from positive wells were removed and propagated. The epitopes recognized by MAb AP33 epitope was mapped to LINTNGSWHIN (412-423) using overlapping peptides. This epitope is highly conserved across all the major genotypes and that MAb AP33 is capable of broad neutralization was demostrated with the retroviral pseudoparticles (HCVpp) assay.</Comments>
</Item><Item><Target_ID> 11</Target_ID>
<Target_Name>Anti-glycoprotein E2 monoclonal antibody 3/11</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Mab 3/11</Synonyms>
<Target_Source>Rattus norvegicus (Rat):10116</Target_Source>
<Target_Structure></Target_Structure>
<Comments>MAb 3/11 was generated from rats after immunization with either baculovirus-expressed E1-E2 complexes or mammalian (human embryonal kidney) cell-expressed E2661 glycoprotein. MAb 3/11 and MAb AP33 recognize distinct yet overlapping epitopes. MAb 3/11 is capable of neutralizing HCVpp carrying strain H77 E1E2.</Comments>
</Item><Item><Target_ID> 12</Target_ID>
<Target_Name>Protein-glutamine gamma-glutamyltransferase 2</Target_Name>
<Target_Type>Protein&gt;Enzyme</Target_Type>
<Target_Sequence>P21980</Target_Sequence>
<Synonyms>Tissue transglutaminase
Transglutaminase C, TGase C, TG(C), TGC
Transglutaminase-2, TGase-2
Transglutaminase H, TGase H
EC=2.3.2.13
</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1KV3, 2Q3Z, 3LY6, 3S3J, 3S3P, 3S3S</Target_Structure>
<Comments>Protein-glutamine gamma-glutamyl transferase 2 catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Reduced TGM2 activity might contribute to disorders of glucose metabolism such as diabetes.</Comments>
</Item><Item><Target_ID> 13</Target_ID>
<Target_Name>Coagulation factor XIII A chain</Target_Name>
<Target_Type>Protein&gt;Enzyme</Target_Type>
<Target_Sequence>P00488</Target_Sequence>
<Synonyms>Coagulation factor XIIIa
Protein-glutamine gamma-glutamyltransferase A chain
Transglutaminase A chain
EC=2.3.2.13</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1EVU, 1EX0, 1F13, 1FIE, 1GGT, 1GGU, 1GGY, 1QRK</Target_Structure>
<Comments>Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.</Comments>
</Item><Item><Target_ID> 14</Target_ID>
<Target_Name>Anti-AMA1 monoclonal antibody 45B1</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Mab 45B1</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure></Target_Structure>
<Comments>The monoclonal antibody 45B1 was produced from mice immunized with the purified P. yoelii yoelii AMA-1 (PyAMA-1). It belongs to the subclass IgG2a. The results of a passive immunization experiment showed that 45B1 protected mice from challenge infection of P. yoelii yoelii YM, with low parasitemias and 100% survival.</Comments>
</Item><Item><Target_ID> 15</Target_ID>
<Target_Name>Anti-P235 rhoptry protein monoclonal antibody 25.77</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Mab 25.77</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure></Target_Structure>
<Comments>Spleen cells from two P. yoelii-immune BALB/c mice were fused with P3-NS1/1-Ag4-1 myeloma cells in the presence of polyethylene glycol. The cells were dispensed into 144 tissue culture wells in 2-ml volumes of hypoxanthine-aminopterine-thymidine-selective  mediums,  using  RPMI-1640  medium supplemented with 10% fetal calf serum as a base. After 10 days, the culture supernatants were tested for P. yoelii-specific antibody by indirect immunofluorescence (IIF). Of 143 cultures tested, 38 were positive, 20 producing antibody apparently directed against the infected erythrocyte membrane and 18 producing antibody against the parasite itself. From the initial screening, five distinct IIF specificities were detected. Cultures representative of each of the IIF specificities were expanded in selective medium without aminopterine, and hybridoma lines were subsequently cloned in semi-solid agar overlayed with medium. Hybridoma 25.77 was one of them. Monoclonal antibody 25.77 belongs to the subclass IgG2a. It was found that 25.77 bound to antigens only present in merozoites, free and within mature schizonts. Later, it was known that this antibody was specific for the P. yoelii yoelii 235-kDa rhoptry protein family. Passive immunization with MAb 25.77 suppressed blood-stage parasitemia and restricted the parasites to reticulocytes.</Comments>
</Item><Item><Target_ID> 16</Target_ID>
<Target_Name>Anti-ochratoxin A monoclonal antibody 10G7</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Mab 10G7</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure></Target_Structure>
<Comments>The anti-ochratoxin A monoclonal antibody 10G7 is an IgG2a, produced from hybridoma based on BALB/c mice immunized with ochratoxin A-KLH conjugates.</Comments>
</Item><Item><Target_ID> 17</Target_ID>
<Target_Name>Vibrio cholerae El Tor Typing Phage VP1</Target_Name>
<Target_Type>Virus</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>Vibrio phage VP1</Synonyms>
<Target_Source>Unclassified phages&gt;Vibrio phage VP1:12333</Target_Source>
<Target_Structure></Target_Structure>
<Comments>VP1 phage was used as one of the typing phages in a phage-biotyping scheme that has been used for nearly 40 years in China for the typing of O1 El Tor strains. Based on the lytic patterns of the five typing phages, El Tor strains can be clustered into 32 phage types.</Comments>
</Item><Item><Target_ID> 18</Target_ID>
<Target_Name>Tumor necrosis factor ligand superfamily member 13B</Target_Name>
<Target_Type>Protein&gt;Others</Target_Type>
<Target_Sequence>Q9Y275</Target_Sequence>
<Synonyms>TNF- and APOL-related leukocyte expressed ligand 1, TALL-1
B lymphocyte stimulator, BLyS
B-cell-activating factor
BAFF
Dendritic cell-derived TNF-like molecule
CD_antigen=CD257</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1KXG, 1JH5, 1KD7, 1OQD, 1OQE, 1OSG, 1OTZ, 3V56</Target_Structure>
<Comments>Tumor necrosis factor ligand superfamily member 13B has two isoforms, i.e. membrane form and soluble form. It abundantly expressed in B cell lineage cells, peripheral blood leukocytes, monocytes and macrophages. This cytokine binds to TNFRSF13B/TACI, TNFRSF17/BCMA and TNFRSF13C/BAFFR, involving in the stimulation of B- and T-cell function and the regulation of humoral immunity.</Comments>
</Item><Item><Target_ID> 19</Target_ID>
<Target_Name>Acetylcholinesterase</Target_Name>
<Target_Type>Protein&gt;Enzyme</Target_Type>
<Target_Sequence>P22303</Target_Sequence>
<Synonyms>AChE
EC=3.1.1.7</Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure>1B41, 1F8U, 1VZJ, 2X8B, 3LII, 4EY4, 4EY5, 4EY6, 4EY7, 4EY8</Target_Structure>
<Comments>Acetylcholinesterase, is an enzyme that degrades the neurotransmitter acetylcholine, producing choline and an acetate group. It is mainly found at neuromuscular junctions and cholinergic nervous system, where its activity serves to terminate synaptic transmission. AChE has a very high catalytic activity - each molecule of AChE degrades about 25000 molecules of acetylcholine per second. Acetylcholinesterase is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen.</Comments>
</Item><Item><Target_ID> 20</Target_ID>
<Target_Name>Anti-aflatoxin B1 monoclonal antibody</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms></Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure></Target_Structure>
<Comments>The isotype of this monoclonal antibody is IgG.</Comments>
</Item><Item><Target_ID> 21</Target_ID>
<Target_Name>Avian infectious bronchitis virus (strain M41)</Target_Name>
<Target_Type>Virus</Target_Type>
<Target_Sequence>GI: 112949615</Target_Sequence>
<Synonyms>IBV</Synonyms>
<Target_Source>Avian infectious bronchitis virus (IBV):11120</Target_Source>
<Target_Structure>3LD1</Target_Structure>
<Comments>Avian infectious bronchitis virus is a coronavirus with a non-segmented, positive-sense single-stranded RNA genome. It infects the respiratory tract, gut, kidney and reproductive systems of chickens.</Comments>
</Item><Item><Target_ID> 22</Target_ID>
<Target_Name>Anti-arginine kinase monoclonal antibody 38G6</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms>MAb 38G6</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure></Target_Structure>
<Comments>The hybridoma 38G6 was established through a fusion of immune splenocytes of a BALB/c mouse immunized with crude cockroach (CR) extract and mouse myeloma cells. It secreted IgG1 monoclonal immunoglobulins. The monoclonal antibody was used in a capture ELISA to detect specific IgE in serum samples of allergic Thai patients. It was found that 72% of the patients had IgE antibodies to the epitope of MAb 38G6 indicating that it was against major CR allergens among the CR allergic Thai patients.</Comments>
</Item><Item><Target_ID> 23</Target_ID>
<Target_Name>Anti-cholera toxin peptide 3 (CTP3) monoclonal antibody TE33</Target_Name>
<Target_Type>Protein&gt;Monoclonal antibody</Target_Type>
<Target_Sequence>GI:494639, GI:494640</Target_Sequence>
<Synonyms>Mab TE33</Synonyms>
<Target_Source>Mus musculus (Mouse):10090</Target_Source>
<Target_Structure>1TET, 1ZEA</Target_Structure>
<Comments>Mab TE33 is an affinity matured murine IgG1 monoclonal antibody raised against cholera toxin peptide 3.</Comments>
</Item><Item><Target_ID> 24</Target_ID>
<Target_Name>Shrimp white spot syndrome virus</Target_Name>
<Target_Type>Virus</Target_Type>
<Target_Sequence>GI:17158105</Target_Sequence>
<Synonyms>Prawn white spot bacilliform virus
White spot syndrome virus of shrimp
White Spot Bacilliform Virus
white spot syndrome virus
white spot syndrome virus of penaeid shrimp
white spot syndrome baculovirus
WSSV</Synonyms>
<Target_Source>White spot syndrome virus (WSSV) (White spot bacilliform virus):92652</Target_Source>
<Target_Structure>2ZUG, 2ED6, 2EDM, 2GJ2, 2GJI</Target_Structure>
<Comments>WSSV is a rod-shaped double-stranded DNA virus, and the size of the enveloped viral particles have been reported to be 240-380 nm long and 70-159 nm dia and nucleocapsid core is 120-205 nm long and 95-165 nm dia. The virus has an outer lipid bilayer membrane envelope, sometimes with a tail like appendage at one end of the virion. Transmission of the virus is mainly through oral ingestion and water borne routes in farms (horizontal transmission) and vertical transmission (from infected mother prawns) in case of shrimp hatcheries. The virus is present in the wild stocks of shrimp, especially in the coastal waters adjacent to shrimp farming regions in Asian countries, but mass mortalities of wild shrimps are yet to be observed.</Comments>
</Item><Item><Target_ID> 25</Target_ID>
<Target_Name>Osteosarcoma cell line OS-732</Target_Name>
<Target_Type>Cell</Target_Type>
<Target_Sequence></Target_Sequence>
<Synonyms></Synonyms>
<Target_Source>Homo sapiens (Human):9606</Target_Source>
<Target_Structure></Target_Structure>
<Comments>The OS-732 tumor cell line was derived from a biopsy obtained before x-ray or Chemotherapy from an osteosarcorna of the distal right femur of a 13-year-old Caucasian girl (M.T.). Despite amputation and treatment with radiation therapy and chemotherapy, she died approximately 3 months later with extensive pulmonary metastases. Autopsy was not performed. OS-732 cells grew to high population density in liquid medium and formed colonies in agar medium. The cell line consisted of polygonal or fusiform cells resembling the cells of the original tumor. No collagen fibers or calcium apatite microcrystals could be demonstrated in the cultured cells by electron microscopy nor were virus particles detected. Isoenzyme studies of the cell line revealed the “B” band of glucose-6-phosphate dehydrogenase. Chromosome studies of the cell line revealed a range of stem line number from 58 to 65; chromosome counts ranged from 47 to 183. Some cells had marker chromosome of varied morphology and some had minute chromosomes. Chromosome breaks were found in 30.5% of the cells (PMID: 5100401).</Comments>
</Item></Target></result>