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hemagglutinin(332-340)[Influenza A virus]
本产品不向个人销售，仅用作科学研究，不用于任何人体实验及非科研性质的动物实验。
hemagglutinin(332-340)[Influenza A virus]图片
包装与价格：
包装价格(元)
1mg电议
5mg电议
10mg电议
25mg电议

产品介绍

Partial antigenic glycoprotein

别名H2N-Thr-Gly-Leu-Arg-Asn-Ile-Pro-Ser-Ile-OH
Canonical SMILESNC(C(C)O)C(NCC(NC(CC(C)C)C(NC(CCCNC(N)=N)C(NC(CC(N)=O)C(NC(C(C)CC)C(N1C(C(NC(CO)C(NC(C(C)CC)C(O)=O)=O)=O)CCC1)=O)=O)=O)=O)=O)=O
分子式C42H75N13O13
分子量970.12
溶解度≥ 97mg/mL in DMSO
储存条件Store at -20℃
General tipsFor obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.
Shipping ConditionEvaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
产品描述

Influenza hemagglutinin (HA) is a type of hemagglutinin found on the surface of the influenza viruses. It is an antigenic glycoprotein. It is responsible for binding the virus to the cell that is being infected. HA proteins bind to cells with sialic acid on the membranes, such as cells in the upper respiratory tract or erythrocytes. [1]
HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of host endosomal membrane with the viral membrane. [2]
Since hemagglutinin is the major surface protein of the influenza A virus and is essential to the entry process, it is the primary target of neutralizing antibodies.


References:
1. Russell RJ, Kerry PS, Stevens DJ, Steinhauer DA, Martin SR, Gamblin SJ, Skehel JJ (November 2008). "Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion". Proc. Natl. Acad. Sci. U.S.A. 105 (46): 17736–41.
2. White JM, Hoffman LR, Arevalo JH, et al. (1997). "Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin". In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.OxfordUniversity Press. pp. 80–104.