产品号 #03804_C
半固体甲基纤维素基杂交瘤筛选和克隆培养基，含HAT（含血清）
概述
通过使用甲基纤维素为基础的培养基一步完成杂交瘤的选择和克隆，节省了研究时间和资源。使用ClonaCell™-HY Medium D容易分离单克隆，单克隆概率高，用于进一步筛选和扩增。
杂交瘤克隆通常具有广泛的生长速率和生产力；当使用ClonaCell™-HY Medium D进行克隆时，它们形成可见且离散的单克隆菌落，防止因过度生长而丢失稀有和高产的克隆。通过人工或机器人的方法，可以很容易地从半固体培养基中挑选杂交瘤菌落，并分散到液体培养基中进行筛选和扩增。
ClonaCell™-HY Medium D是一种半固体培养基，含有血清和选择性试剂次黄嘌呤、氨基蝶呤和胸腺嘧啶（HAT）。它已被证实用于发展小鼠和大鼠杂交瘤。也有报道称，它与使用来自多种宿主动物（包括人类、小鼠、大鼠和仓鼠）的淋巴细胞生产和克隆杂交瘤兼容（例如Wilson JR等）。抗病毒研究，2016)。
为什么使用半固态克隆：
•形成物理上分离的，离散的菌落，可以很容易地分离。
•与散装液体培养相比，在半固体培养基中同时选择和克隆容易分离稀有和高产克隆。
•与限制稀释的选择和克隆相比，用更少的时间和资源分离单克隆细胞系。
找到更多的产品，高效的杂交瘤克隆和一代，在我们的ClonaCell™品牌页面。
Contains
• DMEM
• Methylcellulose
• Serum
• Hypoxanthine, aminopterin, and thymidine (HAT)
• Gentamicin
• 2-Mercaptoethanol
• Phenol red
• L-Glutamine and other supplements
• Other ingredients
Subtype
Semi-Solid Media, Specialized Media
Cell Type
Hybridomas
Species
Human, Mouse, Other, Rat
Application
Cell Culture, Semi-Solid Cloning
Brand
ClonaCell
Area of Interest
Antibody Development, Cancer, Cell Line Development, Drug Discovery and Toxicity Testing, Hybridoma Generation
Formulation Category
Methylcellulose-Based
Protocols and Documentation
Find supporting information and directions for use in the Product Information Sheet or explore additional protocols below.
Applications
This product is designed for use in the following research area(s) as part of the highlighted workflow stage(s). Explore these workflows to learn more about the other products we offer to support each research area.
Resources and Publications
Educational Materials (9)
Frequently Asked Questions
Publications (21)
An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo Antiviral Research 2016 NOV
Abstract
Zoonotic A(H7N9) avian influenza viruses emerged in China in 2013 and continue to be a threat to human public health, having infected over 800 individuals with a mortality rate approaching 40%. Treatment options for people infected with A(H7N9) include the use of neuraminidase (NA) inhibitors. However, like other influenza viruses, A(H7N9) can become resistant to these drugs. The use of monoclonal antibodies is a rapidly developing strategy for controlling influenza virus infection. Here we generated a murine monoclonal antibody (3c10-3) directed against the NA of A(H7N9) and show that prophylactic systemic administration of 3c10-3 fully protected mice from lethal challenge with wild-type A/Anhui/1/2013 (H7N9). Further, post-infection treatment with a single systemic dose of 3c10-3 at either 24, 48 or 72 h post A(H7N9) challenge resulted in both dose- and time-dependent protection of up to 100% of mice, demonstrating therapeutic potential for 3c10-3. Epitope mapping revealed that 3c10-3 binds near the enzyme active site of NA, and functional characterization showed that 3c10-3 inhibits the enzyme activity of NA and restricts the cell-to-cell spread of the virus in cultured cells. Affinity analysis also revealed that 3c10-3 binds equally well to recombinant NA of wild-type A/Anhui/1/2013 and to a variant NA carrying a R289K mutation known to infer NAI resistance. These results suggest that 3c10-3 has the potential to be used as a therapeutic to treat A(H7N9) infections either as an alternative to, or in combination with, current NA antiviral inhibitors.
Immunodominant West Nile virus T cell epitopes are fewer in number and fashionably late The Journal of Immunology 2016 MAY
Abstract
Class I HLA molecules mark infected cells for immune targeting by presenting pathogen-encoded peptides on the cell surface. Characterization of viral peptides unique to infected cells is important for understanding CD8(+) T cell responses and for the development of T cell-based immunotherapies. Having previously reported a series of West Nile virus (WNV) epitopes that are naturally presented by HLA-A*02:01, in this study we generated TCR mimic (TCRm) mAbs to three of these peptide/HLA complexes-the immunodominant SVG9 (E protein), the subdominant SLF9 (NS4B protein), and the immunorecessive YTM9 (NS3 protein)-and used these TCRm mAbs to stain WNV-infected cell lines and primary APCs. TCRm staining of WNV-infected cells demonstrated that the immunorecessive YTM9 appeared several hours earlier and at 5- to 10-fold greater density than the more immunogenic SLF9 and SVG9 ligands, respectively. Moreover, staining following inhibition of the TAP demonstrated that all three viral ligands were presented in a TAP-dependent manner despite originating from different cellular compartments. To our knowledge, this study represents the first use of TCRm mAbs to define the kinetics and magnitude of HLA presentation for a series of epitopes encoded by one virus, and the results depict a pattern whereby individual epitopes differ considerably in abundance and availability. The observations that immunodominant ligands can be found at lower levels and at later time points after infection suggest that a reevaluation of the factors that combine to shape T cell reactivity may be warranted.
Deletion of a Yci1 Domain Protein of Candida albicans Allows Homothallic Mating in MTL Heterozygous Cells mBio 2016 MAY
Abstract
It has been proposed that the ancestral fungus was mating competent and homothallic. However, many mating-competent fungi were initially classified as asexual because their mating capacity was hidden behind layers of regulation. For efficient in vitro mating, the essentially obligate diploid ascomycete pathogen Candida albicans has to change its mating type locus from heterozygous MTL a /α to homozygous MTL a / a or MTL α/α and then undergo an environmentally controlled epigenetic switch to the mating-competent opaque form. These requirements greatly reduce the potential for C. albicans mating. Deletion of the Yci1 domain gene OFR1 bypasses the need for C. albicans cells to change the mating type locus from heterozygous to homozygous prior to switching to the opaque form and mating and allows homothallic mating of MTL heterozygous strains. This bypass is carbon source dependent and does not occur when cells are grown on glucose. Transcriptional profiling of ofr1 mutant cells shows that in addition to regulating cell type and mating circuitry, Ofr1 is needed for proper regulation of histone and chitin biosynthesis gene expression. It appears that OFR1 is a key regulator in C. albicans and functions in part to maintain the cryptic mating phenotype of the pathogen.
更多信息
| Species | Human, Mouse, Other, Rat |
|---|---|
| Contains | • DMEM • Methylcellulose • Serum • Hypoxanthine, aminopterin, and thymidine (HAT) • Gentamicin • 2-Mercaptoethanol • Phenol red • L-Glutamine and other supplements • Other ingredients |
| Formulation Category | Methylcellulose-Based |
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PRODUCTS ARE FOR RESEARCH USE ONLY AND NOT INTENDED FOR HUMAN OR ANIMAL DIAGNOSTIC OR THERAPEUTIC USES UNLESS OTHERWISE STATED. FOR ADDITIONAL INFORMATION ON QUALITY AT STEMCELL, REFER TO WWW.STEMCELL.COM/COMPLIANCE. Safety Statement: CA WARNING: This product can expose you to Aminopterin which is known to the State of California to cause birth defects or other reproductive harm. For more information go to www.P65Warnings.ca.gov
