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SAB2702196

Sigma-Aldrich

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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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43

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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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)
Qianying Hu et al.
The EMBO journal, 42(1), e110937-e110937 (2022-11-17)
Hutchinson-Gilford progeria syndrome (HGPS) is a lethal premature aging disorder without an effective therapeutic regimen. Because of their targetability and influence on gene expression, microRNAs (miRNAs) are attractive therapeutic tools to treat diseases. Here we identified that hsa-miR-59 (miR-59) was
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)
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)

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