Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place. .; Determines the virion''s shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms. .

q20nv9, q76v02, q76v05, q08ig8, q76v03, q20pm1, q77w48, q20p02, q0a457

Matrix protein 1 (M1),M,matrix protein 1, M1

Influenza A virus (A/mallard/Sweden/6148/2005 (H10N7))

WB,IHC,ELISA

WB 1:500-1:2000
IHC 1:50-1:300
ELISA 1:5000-1:20000

28kD

Rabbit

Recombinant Influenza A virus (Flu A/H10N7) Matrix protein 1 (Met1-Gln158).

Polyclonal

IgG

Antigen affinity purification.

0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.