SAB2702196
Monoclonal Anti-HA tag antibody produced in mouse
clone GT423, affinity isolated antibody
Synonym(s):
Anti-HA Antibody, HA Tag Detection Antibody, Mouse Anti-HA Tag
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All Photos(4)
About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
Recommended Products
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
GT423, monoclonal
form
buffered aqueous solution
concentration
1mg/mL
technique(s)
immunoprecipitation (IP): suitable
indirect immunofluorescence: suitable
western blot: 1000-10000
isotype
IgG2b
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
The hemagglutinin (HA) gene is mapped to segment 4 of Influenza B viral genome. HA is a dominant antigen present on the influenza viral surface. HA is a homotrimer, in which each monomer is produced as a single polypeptide. This monomer is cleaved into two subunits HA1 and HA2 by the host protease. Influenza hemagglutinin protein is a nona-peptide derived from the major spike membrane glycoprotein of the human influenza virus. This strain specific glycoprotein is a homotrimer of 84kDa monomers.
Immunogen
The immunogen used to generate this antibody corresponds to HA tag
Application
Suggested starting dilutions are as follows: ICC/IF: 1:100-1:2000, IP: 1:100-1:500, WB: 1:1000-1:10000. Not yet tested in other Application Longs. Optimal working dilutions should be determined experimentally by the end user.Monoclonal Anti-HA tag antibody produced in mouse has been used in western blot analysis.
Biochem/physiol Actions
Hemagglutinin (HA) is an influenza-virus glycoprotein that regulates membrane fusion and receptor-binding functions during viral entry and infection. The virus gains entry into the host cell via endocytosis and successive membrane fusion mediated by the HA antigen. HA plays a crucial role in viral pathogenesis and host response to viral infection.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Other Notes
Purification: Affinity purified by Protein G
Physical form
Phosphate-buffered saline, no preservative added.
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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Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
MTOPVIB interacts with AtPRD1 and plays important roles in formation of meiotic DNA double-strand breaks in Arabidopsis
Tang Y, et al.
Scientific Reports, 7(1), 10007-10007 (2017)
Functional evaluation of Dent?s disease-causing mutations: implications for ClC-5 channel trafficking and internalization.
Ludwig M, et al.
Human Genetics, 117(2-3), 228-237 (2005)
A potent anti-influenza compound blocks fusion through stabilization of the prefusion conformation of the hemagglutinin protein.
White K M, et al.
ACS infectious diseases, 1(2), 98-109 (2014)
Yu Tang et al.
Scientific reports, 7(1), 10007-10007 (2017-09-01)
Meiotic recombination is initiated from the formation of DNA double-strand breaks (DSBs). In Arabidopsis, several proteins, such as AtPRD1, AtPRD2, AtPRD3, AtDFO and topoisomerase (Topo) VI-like complex, have been identified as playing important roles in DSB formation. Topo VI-like complex
On the origin of the human influenza virus subtypes H2N2 and H3N2.
Scholtissek C, et al.
Virology, 87(1), 13-20 (1978)
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