A4404
Anti-Arachis hypogaea Lectin antibody produced in rabbit
fractionated antiserum, lyophilized powder
别名:
Anti-PNA, Anti-Peanut Lectin
biological source
rabbit
conjugate
unconjugated
antibody form
fractionated antiserum
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
packaging
vial of ~2 mL Lyophilized antiserum
technique(s)
indirect ELISA: 1:80,000
storage temp.
2-8°C
Quality Level
General description
Arachis hypogaea Lectin or peanut lectin (PNA) is known to function as a marker for intercalated cells in rats. PNA also binds to glycoproteins present in human epidermal keratinocytes. Thus, anti-PNA antibodies are often used for protein localization and immunoprecipitation assays of PNA-binding cells or proteins. Rabbit Anti-Arachis hypogaea Lectin antibody binds to Arachis hypogaea lectin.
Immunogen
Peanut lectin (PNA)
Application
Mouse myotube cultures were ran on SDS page gels and membranes treated with PNA for 24hrs the probed with anti-PNA anitbody at a 1:10 dilution.
Rabbit Anti-Arachis hypogaea Lectin antibody can be used for Ouchterlony double diffusion (1:8) assays.
Physical form
Lyophilized from 0.01 M phosphate buffered saline, pH 7.2.
Preparation Note
Reconstitute with 2 mL deionized water.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
S Keeble et al.
Differentiation; research in biological diversity, 43(2), 139-145 (1990-04-01)
We have previously shown that peanut lectin (PNA) binding is a useful marker of keratinocyte terminal differentiation and have identified two PNA-binding glycoproteins with electrophoretic mobilities of approximately 250 kDa and 110 kDa [11]. We now report that in epidermis
Monu Goel et al.
American journal of physiology. Renal physiology, 290(5), F1241-F1252 (2005-11-24)
It is well established that transient receptor potential (TRP) channels are activated following stimulation of G protein-coupled membrane receptors linked to PLC, but their differential expression in various cells of the renal nephron has not been described. In the present
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