Product Details

Purity

>85% (SDS-PAGE)

Target Names

Uniprot No.

Q9Q0U6

Alternative Names

HA; Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]

Species

Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.

Gene References into Functions

Positions 380-461 and 483-565 of HA were novel antigenic epitopes in mouse and chicken. PMID: 29869036
a single nucleotide substitution, resulting in a change from Gly to Asp at position 225 (G225D), completely switches HA specificity to human-type (NeuAcalpha2-6Gal) receptors. PMID: 28694323
results showed that a variety of HA variants emerged during single-virus infections of human airway cells, with variant HA properties selected for fitness for human cell infection. PMID: 29563293
Data suggest that expansion of the vaccine hemagglutinin (HA) subunit 1 (HA1) 3D model database will improve international emergency responses to avian influenza virus (AIV). PMID: 28375167
Glycosylation of the HA of avian influenza H5N1 modulates virus replication, virulence and chicken-to-chicken transmission. PMID: 27902339
Addition of N-glycosylation sites on the globular head of the H5 hemagglutinin induces the escape of immunity. PMID: 26433051
K193E and G225E mutations of HA synergistically attenuated H5N1 virus without enhancing the receptor-binding avidity. PMID: 25998916
The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature. PMID: 25398882
Probe structure-function properties of the H5 hemagglutinin stem loop region by site-directed mutagenesis. Most mutations do not disrupt expression, proteolytis, incorporation into virus, or receptor binding; but many mutations disrupt the entry process. PMID: 24947513
The growth of H5N1 avian influenza viruses is affected by changes of glycosylation sites in HA protein. PMID: 24386837
D53, Y274, E83a, and N276 in HA are conserved neutralization epitope identified by H5M9 antibody. PMID: 24049169
Studies indicate that antigenic drift mutations in immune-dominant regions on the hemagglutinin (HA) structure allow the virus to escape neutralizing antibody (Ab) neutralization. PMID: 23933511
Parainfluenza virus 5 mutants expressing hemagglutinin HA from H5N1 virus induced the highest levels of anti-HA antibodies, the strongest T cell responses, and the best protection against an H5N1 lethal challenge in mice. PMID: 23804633
A single, acid-stabilizing mutation enhanced growth of virus in upper respiratory tract, yet was insufficient to enable transmission in ferrets in the absence of mutations for alpha(2,6) receptor binding specificity and that remove a glycosylation site. PMID: 23824818
Increasing the pH stability of the H5 HA resulted in increased viral shedding of H5N1 from the nasal cavity of ferrets. PMID: 23486663
The pH of activation of the HA protein regulates H5N1 influenza virus replication and pathogenesis. PMID: 23449784
a single residue substitution in the receptor-binding domain of H5N1 hemagglutinin is critical for packaging into pseudotyped lentiviral particles PMID: 23133587
the HA 3' NCR sequence of NIBRG-14 is different to that of the parental wild type virus A/Vietnam/1194/2004; however this does not appear to impact on its growth or antigen yield PMID: 22606247
The hemagglutinin cleavage site contributes to the pathogenicity of H5N1 influenza virus. PMID: 22496231
Expression of NS1 in trans rescues HA protein and mRNA expression from NS1-truncated viruses. PMID: 22398291
The multibasic cleavage site in HA is critical for virus spread along the olfactory and hematogenous routes in ferret model. PMID: 22278228
The multibasic cleavage site of the hemagglutinin acts as a virulence factor in a host-specific manner in mammals. PMID: 22205751
Only the HA, and not the NS, gene from the 2004 H5N1 virus induces IL-1beta, MIP-lalpha, IL-8 and IL-18 cytokine productions from activated U937 cells PMID: 22299315
analysis of a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide PMID: 21994935
Mutation at position 90 and 160 in the hemagglutinin determine avian-to-human interspecies transmission. PMID: 21744000
Mutations in the receptor binding domain of HA did not increase the transmissibility of avian influenza H5N1 viruses to human cell. PMID: 21397290
HA proteins of H1N1 and H5N1 influenza A viruses activated dendritic cells. PMID: 20844030
Mutations within HA 219-240 region at the position D239 (D239E/G/N) are reported with higher frequency. PMID: 20160492
Five of the antibodies which showed binding to the relatively conserved HA2 subunit of HA, exhibited neutralization of H5N1-VLP uptake in a dose dependant manner PMID: 18957074
A highly conserved mimotope is present in HA of various H5N1 subtypes. PMID: 19226949
One double mutation (V135S and A138S) in hemagglutinin significantly enhances alpha-2,6-linked receptor recognition by the H5 subtype. PMID: 19399777
Results demonstrate the existence of immunodominant positions in the H5 HA protein, alteration of these residues might improve the immunogenicity of vaccine strains. PMID: 19798682
analysis of HA sequences revealed that the peptide sequences around the glycosylation sites are highly conserved, which suggests a central functional significance for HA glycosylation PMID: 19822741

Hide All

Subcellular Location

Virion membrane; Single-pass type I membrane protein. Host apical cell membrane; Single-pass type I membrane protein.

Protein Families

Influenza viruses hemagglutinin family

Database Links

KEGG: vg:3654620

Message

Product >> Product Name：
Product >> Code：
Name： *
Email： *
Company/Organization：
Phone：
Since emails may get flagged by spam filters occasionally, we recommend leaving your phone number as a precaution. Your information is safe with us.
Question/Comment： *
Your Region： *
I'd like to receive email newsletters from Cusabio

Yes

No
How do you know CUSABIO?

Email

Distributor

Search engine

Advertisement

Others
CAPTCHA verification：

Code	CSB-YP879396IEF
MSDS	MSDS
Size	Pls inquire
Source	Yeast
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP879396IEF
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-EP879396IEF-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-BP879396IEF
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
Have Questions?	Leave a Message or Start an on-line Chat

Code	CSB-MP879396IEF
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
Have Questions?	Leave a Message or Start an on-line Chat

Recombinant Influenza A virus Hemagglutinin (HA), partial

Product Details

Customer Reviews and Q&A

Target Background

×CloseMessage