产品号 #03831_C
Hybridoma selection medium, with HAT (serum-containing)
概述
ClonaCell™-HY Liquid HAT Selection Medium is a serum-containing medium with hypoxanthine, aminopterin, and thymidine (HAT) for the selection of hybridomas following the fusion of lymphocytes and myeloma cells. This medium has been verified for use in mouse and rat hydridoma development and reportedly is compatible for production and cloning of myelomas and/or hybridomas using lymphocytes from a variety of host animals including human, mouse, rat, and hamster.
Contains
• DMEM
<br> • Serum
<br> • Hypoxanthine, aminopterin, and thymidine (HAT)
<br> • Gentamicin
<br> • 2-Mercaptoethanol
<br> • Phenol red
<br> • L-Glutamine and other supplements
<br> • Other ingredients
Subtype
Specialized Media
Cell Type
Hybridomas
Species
Mouse
Application
Cell Culture, Hybridoma Generation
Brand
ClonaCell
Area of Interest
Antibody Development, Cell Line Development, Drug Discovery and Toxicity Testing, Hybridoma Generation
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 (1)
Frequently Asked Questions
Publications (6)
Characterization of an enhanced antigenic change in the pandemic 2009 H1N1 influenza virus haemagglutinin Journal of General Virology 2014
Abstract
Murine hybridomas producing neutralizing mAbs specific to the pandemic influenza virus A/California/07/2009 haemagglutinin (HA) were isolated. These antibodies recognized at least two different but overlapping new epitopes that were conserved in the HA of most Spanish pandemic isolates. However, one of these isolates (A/Extremadura/RR6530/2010) lacked reactivity with the mAbs and carried two unique mutations in the HA head (S88Y and K136N) that were required simultaneously to eliminate reactivity with the murine antibodies. This unusual requirement directly illustrates the phenomenon of enhanced antigenic change proposed previously for the accumulation of simultaneous amino acid substitutions at antigenic sites of the influenza A virus HA during virus evolution (Shih et al., Proc Natl Acad Sci USA, 104 , 6283-6288, 2007). The changes found in the A/Extremadura/RR6530/2010 HA were not found in escape mutants selected in vitro with one of the mAbs, which contained instead nearby single amino acid changes in the HA head. Thus, either single or double point mutations may similarly alter epitopes of the new antigenic site identified in this work in the 2009 H1N1 pandemic virus HA. Moreover, this site is relevant for the human antibody response, as shown by competition of mAbs and human post-infection sera for virus binding. The results are discussed in the context of the HA antigenic structure and challenges posed for identification of sequence changes with possible antigenic impact during virus surveillance.
Isolation of mouse pancreatic alpha, beta, duct and acinar populations with cell surface markers Molecular and Cellular Endocrinology 2011 JUN
Abstract
Tools permitting the isolation of live pancreatic cell subsets for culture and/or molecular analysis are limited. To address this, we developed a collection of monoclonal antibodies with selective surface labeling of endocrine and exocrine pancreatic cell types. Cell type labeling specificity and cell surface reactivity were validated on mouse pancreatic sections and by gene expression analysis of cells isolated using FACS. Five antibodies which marked populations of particular interest were used to isolate and study viable populations of purified pancreatic ducts, acinar cells, and subsets of acinar cells from whole pancreatic tissue or of alpha or beta cells from isolated mouse islets. Gene expression analysis showed the presence of known endocrine markers in alpha and beta cell populations and revealed that TTR and DPPIV are primarily expressed in alpha cells whereas DGKB and GPM6A have a beta cell specific expression profile.
Essential role of TNF receptor superfamily 25 (TNFRSF25) in the development of allergic lung inflammation The Journal of Experimental Medicine 2008 MAY
Abstract
We identify the tumor necrosis factor receptor superfamily 25 (TNFRSF25)/TNFSF15 pair as critical trigger for allergic lung inflammation, which is a cardinal feature of asthma. TNFRSF25 (TNFR25) signals are required to exert T helper cell 2 (Th2) effector function in Th2-polarized CD4 cells and co-stimulate interleukin (IL)-13 production by glycosphingolipid-activated NKT cells. In vivo, antibody blockade of TNFSF15 (TL1A), which is the ligand for TNFR25, inhibits lung inflammation and production of Th2 cytokines such as IL-13, even when administered days after airway antigen exposure. Similarly, blockade of TNFR25 by a dominant-negative (DN) transgene, DN TNFR25, confers resistance to lung inflammation in mice. Allergic lung inflammation-resistant, NKT-deficient mice become susceptible upon adoptive transfer of wild-type NKT cells, but not after transfer of DN TNFR25 transgenic NKT cells. The TNFR25/TL1A pair appears to provide an early signal for Th2 cytokine production in the lung, and therefore may be a drug target in attempts to attenuate lung inflammation in asthmatics.
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
