Influenza NP 147-155
目录号 : GC36317
Influenza NP (147-155) 是一种源于流感核蛋白的 Kd 限制性表位。
Cas No.:132326-72-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Influenza NP (147-155) is a Kd restricted epitope from influenza nucleoprotein[1].
[1]. Ikonomidis G, et al. Influenza-specific immunity induced by recombinant Listeria monocytogenes vaccines. Vaccine. 1997 Mar;15(4):433-40.
| Cas No. | 132326-72-8 | SDF | |
| 分子式 | C48H82N16O14 | 分子量 | 1107.26 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.9031 mL | 4.5157 mL | 9.0313 mL |
| 5 mM | 0.1806 mL | 0.9031 mL | 1.8063 mL |
| 10 mM | 0.0903 mL | 0.4516 mL | 0.9031 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Re-evaluating the generation of a "proteasome-independent" MHC class I-restricted CD8 T cell epitope
J Immunol 2006 Feb 15;176(4):2249-61.PMID:16455981DOI:10.4049/jimmunol.176.4.2249.
The proteasome is primarily responsible for the generation of MHC class I-restricted CTL epitopes. However, some epitopes, such as NP(147-155) of the influenza nucleoprotein (NP), are presented efficiently in the presence of proteasome inhibitors. The pathways used to generate such apparently "proteasome-independent" epitopes remain poorly defined. We have examined the generation of NP(147-155) and a second proteasome-dependent NP epitope, NP(50-57), using cells adapted to growth in the presence of proteasome inhibitors and also through protease overexpression. We observed that: 1) Ag processing and presentation proceeds in proteasome-inhibitor adapted cells but may become more dependent, at least in part, on nonproteasomal protease(s), 2) tripeptidyl peptidase II does not substitute for the proteasome in the generation of NP(147-155), 3) overexpression of leucine aminopeptidase, thymet oligopeptidase, puromycin-sensitive aminopeptidase, and bleomycin hydrolase, has little impact on the processing and presentation of NP(50-57) or NP(147-155), and 4) proteasome-inhibitor treatment altered the specificity of substrate cleavage by the proteasome using cell-free digests favoring NP(147-155) epitope preservation. Based on these results, we propose a central role for the proteasome in epitope generation even in the presence of proteasome inhibitors, although such inhibitors will likely alter cleavage patterns and may increase the dependence of the processing pathway on postproteasomal enzymes.
Creating CTL targets with epitope-linked beta 2-microglobulin constructs
J Immunol 1998 Feb 15;160(4):1598-605.PMID:9469415doi
Eliciting a strong CTL response is dependent upon displaying suitably high levels of specific class I MHC/peptide complexes at the cell surface. In an effort to enhance the presentation of defined CTL target structures, two unique peptide-linked beta 2-microglobulin (beta 2m) molecules were constructed. The first, designated NP(366-374)-L8-h beta 2m, links the carboxyl terminus of the H-2Db-restricted influenza nucleoprotein (NP) epitope NP(366-374) to the amino terminus of h beta 2m through an eight-amino acid glycine/serine linker. The second molecule, designated NP(147-155)-L12-h beta 2m, similarly couples the H-2Kd-restricted influenza NP epitope NP(147-155) to h beta 2m via a 12-residue polypeptide linker. Transfection of the NP(366-374)-L8-h beta 2m vector into H-2b-expressing cell lines sensitized these cells for lysis by NP(366-374)-specific CTLs. Free NP peptide could not be detected when class I bound peptides were acid-extracted from the surface of NP(366-374)-L8-h beta2m transfectants, indicating that CTL killing was mediated by recognition of the peptide linked to h beta 2m and not by a degradation by-product. CTL target structure formation was also achieved by an exogenous presentation pathway. H-2d-expressing target cells were sensitized for lysis when pulsed with NP(147-155)-L12-h beta 2m protein derived from an Escherichia coli cell lysate. The effect of recombinant NP(147-155)-L12-h beta 2m was inhibited by competitor wild-type h beta 2m, indicating that the active peptide-h beta 2m fusion protein remained intact. The observation that beta 2m with covalently attached peptide can effectively create CTL target structures in vitro offers new possibilities for the in vivo induction of epitope-specific CTL responses by either DNA immunization or injection of the purified epitope-linked beta 2m.
Enhanced protective immunity against H5N1 influenza virus challenge by vaccination with DNA expressing a chimeric hemagglutinin in combination with an MHC class I-restricted epitope of nucleoprotein in mice
Antiviral Res 2009 Mar;81(3):253-60.PMID:19135483DOI:10.1016/j.antiviral.2008.12.009.
DNA vaccination is an effective means of eliciting both humoral and cellular immune responses. The hemagglutinin (HA) surface protein of influenza A virus is a major target of protective antibody responses induced by virus infection or by vaccination and is widely considered to be the antigen of choice for an influenza vaccine. Cytotoxic T lymphocyte (CTL) responses directed against the conserved nucleoprotein (NP) are thought to play an important role in clearing virus and promoting survival and recovery from influenza. In this study, we developed a novel DNA vaccine approach using a chimeric plasmid consisting of the HA of H5N1 influenza virus in which an MHC class I-restricted NP-specific CTL epitope (NP147-155) was inserted. Immunogenicity and antiviral efficacy of this vaccine was assessed in mouse models. A similar level of HA expression was achieved in 293T cells transfected with pHA/NP(147-155) compared to that with pHA. Besides eliciting the specific anti-HA antibody responses, vaccination using pHA/NP(147-155) in mice induced NP epitope-specific CD8(+) T cell responses, which are generally not inducible by vaccination with pHA alone. After H5N1 influenza virus challenge, BALB/c mice vaccinated with pHA/NP(147-155) exhibited reduced inflammation severity and lung viral titers compared to those vaccinated with pHA. Our work may contribute to improvement of HA-based influenza DNA vaccines.
Primary pulmonary cytotoxic T lymphocytes induced by immunization with a vaccinia virus recombinant expressing influenza A virus nucleoprotein peptide do not protect mice against challenge
J Virol 1994 Jun;68(6):3505-11.PMID:7514677DOI:10.1128/JVI.68.6.3505-3511.1994.
The nucleoprotein (NP) of influenza A virus is the dominant antigen recognized by influenza virus-specific cytotoxic T lymphocytes (CTLs), and adoptive transfer of NP-specific CTLs protects mice from influenza A virus infection. BALB/c mouse cells (H-2d) recognize a single Kd-restricted CTL epitope of NP consisting of amino acids 147 to 155. In the present study, mice were immunized with various vaccinia virus recombinant viruses to examine the effect of the induction of primary pulmonary CTLs on resistance to challenge with influenza A/Puerto Rico/8/34 virus. The minigene ESNP(147-155)-VAC construct, composed of a signal sequence from the adenovirus E3/19K glycoprotein (designated ES) and expressing the 9-amino-acid NP natural determinant (amino acids 147 to 155) preceded by an alanine residue, a similar minigene NP(Met 147-155)-VAC lacking ES, and a full-length NP-VAC recombinant of influenza virus were analyzed. The two minigene NP-VAC recombinants induced a greater primary pulmonary CTL response than the full-length NP-VAC recombinant. However, NP-specific CTLs induced by immunization with ESNP(147-155)-VAC did not decrease peak virus titer or accelerate clearance of virus in the lungs of mice challenged intranasally with A/PR/8/34. Furthermore, NP-specific CTLs induced by immunization did not protect mice challenged intranasally with a lethal dose of A/PR/8/34. Sequence analysis of the NP CTL epitope of A/PR/8/34 challenge virus obtained from lungs after 8 days of replication in ESNP(147-155)-VAC-immunized mice showed identity with that of the input virus, demonstrating that an escape mutant had not emerged during replication in vivo. Thus, in contrast to adoptively transferred CTLs, pulmonary NP-specific CTLs induced by recombinant vaccinia virus immunization do not have protective in vivo antiviral activity against influenza virus infection.
Influenza-specific immunity induced by recombinant Listeria monocytogenes vaccines
Vaccine 1997 Mar;15(4):433-40.PMID:9141215DOI:10.1016/s0264-410x(96)00188-0.
In this study, we evaluate two Listeria monocytogenes strains that express influenza nucleoprotein (NP) sequences for their ability to protect against challenge with influenza-virus. The construction of one strain, which expresses only the Kd restricted NP epitope (NP 147-155), is described in this study; the other strain, which expresses the full NP sequence in the form of a fusion protein, has been described previously. The ability of the two strains to present the Kd restricted NP epitope in vitro and induce NP-specific CTL in vivo is also described. Mice immunized by the intravenous route with either strain cleared a subsequent (3 weeks post-immunization) influenza virus infection more rapidly as indicated by reduced virus titers in the lungs 5 days after challenge. Efficacy of both recombinant L. monocytogenes strains as vaccines in this system was equivalent and equal to that of recombinant vaccinia expressing NP.