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Merck
모든 사진(4)

문서

SAB2702196

Sigma-Aldrich

Monoclonal Anti-HA tag antibody produced in mouse

clone GT423, affinity isolated antibody

동의어(들):

Anti-HA Antibody, HA Tag Detection Antibody, Mouse Anti-HA Tag

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About This Item

UNSPSC 코드:
12352203
NACRES:
NA.43

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

GT423, monoclonal

형태

buffered aqueous solution

농도

1mg/mL

기술

immunoprecipitation (IP): suitable
indirect immunofluorescence: suitable
western blot: 1000-10000

동형

IgG2b

배송 상태

wet ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

일반 설명

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.

면역원

The immunogen used to generate this antibody corresponds to HA tag

애플리케이션

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.

생화학적/생리학적 작용

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.

특징 및 장점

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.

기타 정보

Purification: Affinity purified by Protein G

물리적 형태

Phosphate-buffered saline, no preservative added.

면책조항

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


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리 방문

Yu Tang et al.
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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
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)
Long Liu et al.
Infectious agents and cancer, 17(1), 52-52 (2022-10-05)
Hepatitis B virus (HBV) causes acute and chronic infection in the clinic. Hepatocellular carcinoma (HCC) is closely linked to HBV infection. Serum Golgi protein 73 (GP73) increases during HBV infection. However, the role of GP73 during HBV infection and the
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
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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