Product Details

Purity

>85% (SDS-PAGE)

Target Names

SNF7

Uniprot No.

P39929

Alternative Names

SNF7; DID1; VPS32; YLR025WVacuolar-sorting protein SNF7; DOA4-independent degradation protein 1; Sucrose nonfermenting protein 7; Vacuolar protein-sorting-associated protein 32

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Expression Region

1-240

Target Protein Sequence

MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE ARIFLTKGNK VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN LETMRAMQEG AKAMKTIHSG LDIDKVDETM DEIREQVELG DEISDAISRP LITGANEVDE DELDEELDML AQENANQETS KIVNNNVNAA PISENKVSLP SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL

Protein Length

full length protein

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.

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

Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting. Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen. ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface. Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces. SNF7 filaments then form spirals that could function as spiral springs. The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission. SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles. ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly.

Gene References into Functions

The major ESCRT-III subunit Snf7 localizes transiently to vesicles and tubules surrounded by a cup-shaped membrane and this was accelerated in vps4Delta cells, correlating with increased Acb1 secretion. PMID: 27115345
Novel mutations has been characterized in ESCRT-III Snf7 that trigger activation, and a novel role have been assigned to Bro1, the yeast ALIX ortholog, in Snf7 assembly. PMID: 27074665
Using a combination of biochemical and genetic approaches, both in vitro and in vivo, we demonstrate that mutations on these protein interfaces halt Snf7 assembly and block endosomal sorting complexes required for transport function. PMID: 26670543
Snf7 alpha6 helix is crucial for binding of Bro1 and Rim20 in vivo and is indispensable for the multivesicular body sorting. PMID: 24058170
Binding of Vps4 to ESCRT-III, coordinated by interactions with Vps2 and Snf7, is coupled to membrane neck constriction during intraluminal vesicle formation. PMID: 24711499
we demonstrate that the N terminus of Snf7 has been tuned to maintain the topological constraints associated with ESCRT-III-filament-mediated membrane invagination and vesicle formation. PMID: 24139821
A rns4/vps32 mutation on the RNase T1 expression-sensitive strain of Saccharomyces Cerevisiae provides evidence for altered ambient response resulting in transportation of the secretory protein to vacuoles. PMID: 15925308
Snf7 influences SUC2 gene expression through activation of the Rim101 pathway. PMID: 18806212
By generating SNF7 mutations that severely affect endocytic trafficking, but leave the Rim pathway function intact, data show that the two functions of SNF7 can be separated genetically. PMID: 19725809

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Subcellular Location

Cytoplasm. Endosome membrane; Peripheral membrane protein. Nucleus envelope.

Protein Families

SNF7 family

Database Links

KEGG: sce:YLR025W

STRING: 4932.YLR025W

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Recombinant Saccharomyces cerevisiae Vacuolar-sorting protein SNF7 (SNF7)

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