Recombinant Human Vacuolar Protein Sorting-Associated Protein 4A (VPS4A) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00724P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Vacuolar Protein Sorting-Associated Protein 4A (VPS4A) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00724P
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Product Overview

Description Recombinant Human Vacuolar Protein Sorting-Associated Protein 4A (VPS4A) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9UN37
Target Symbol VPS4A
Synonyms (Protein SKD2)(VPS4-1)(hVPS4)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCVQYLDRAEKLKDYLRSKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIHELARKTEGYSGADISIIVRDSLMQPVRKVQSATHFKKVCGPSRTNPSMMIDDLLTPCSPGDPGAMEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFGQES
Expression Range 1-437aa
Protein Length Full Length
Mol. Weight 53.9 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan.; (Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses).
Subcellular Location Late endosome membrane; Peripheral membrane protein. Midbody.
Protein Families AAA ATPase family
Database References

HGNC: 13488

OMIM: 609982

KEGG: hsa:27183

STRING: 9606.ENSP00000254950

UniGene: PMID: 28349933

  • Continuous ESCRT-III remodelling by dynamic subunit turnover is regulated by Vps4 to mediate membrane remodelling during cytokinesis. PMID: 28604678
  • associations were noted between the striatal node, hyperactivity, and the vacuolar protein sorting-associated protein 4A (VPS4A) gene in humans, and the causal role of Vps4 for hyperactivity was validated in Drosophila PMID: 27001827
  • These results point to the existence of previously undetected biological functions of the FTase alpha subunit that includes control of intracellular membrane trafficking. PMID: 26551458
  • these experiments suggest that miR-16 and VPS4a expression are altered in end-stage heart failure and in response to unloading with a left ventricular assist device PMID: 25033200
  • Ca2+-dependent accumulation of ESCRT III-Vps4 complex following large focal injury to the cell membrane and identify the role of ALG-2 as the initiator of sequential ESCRT III-Vps4A/B complex assembly. PMID: 25534348
  • Vps4A may function as a tumor suppressor, which utilizes exosomes as mediators to regulate the secretion and uptake of miRNAs in hepatoma cells; these observations provide new insights into the development of HCC. PMID: 25503676
  • Vps4 stimulatory element of the cofactor Vta1 contacts the ATPase Vps4 alpha7 and alpha9 subunits to stimulate ATP hydrolysis. PMID: 25164817
  • Propose that the abscission checkpoint is mediated by ANCHR and CHMP4C through retention of VPS4 at the midbody ring. PMID: 24814515
  • VPS4 is required for endosomal transport of LDL cholesterol in HeLa cells. PMID: 23009658
  • silencing CHMP6 and VPS4A also blocked epidermal growth factor receptor (EGFR) recycling PMID: 22231449
  • VPS4, a master regulator of MVB sorting, may serve as a determinant of lysosomal targeting or extracellular secretion of alphaSYN and thereby contribute to the intercellular propagation of Lewy pathology in PD PMID: 22216284
  • These results indicate that VPS4A has a direct role in membrane scission leading to HIV-1 release. PMID: 21394086
  • Findings reveal new ways in which VPS4 activity is regulated and specifically directed to ESCRT-III polymers. PMID: 20805225
  • It was found that neither siRNA knockdown of VPS4A and VPS4B expression nor the use of cell lines that inducibly express VPS4A or VPS4B dominant negative mutants, inhibited influenza virus budding. PMID: 20621136
  • ESCRT-III/VPS4 proteins function at centrosomes to help regulate their maintenance or proliferation and then at midbodies during abscission, thereby helping ensure the ordered progression through the different stages of cell division. PMID: 20616062
  • Vps4 and the ESCRT-III complex are required for the release of infectious hepatitis C virus particles. PMID: 19828764
  • SKD1-dependent endosomal membrane trafficking is required for formation of autolysosomes. PMID: 11937716
  • Data suggested that hVPS4 is involved in the release of components of the bilayered coat from the endosomal membrane. PMID: 15075231
  • hSnf7-1 binds to itself, membranes, and the AAA+ ATPase SKD1 PMID: 15632132
  • The solution structure of the N-terminal VPS4A microtubule interacting and transport (MIT) domain was reported. PMID: 16174732
  • in cells expressing dominant negative VPS4a, doxorubicin accumulates in VPS4a-positive vesicles and drug sequestration is inhibited PMID: 16841193
  • Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPase-defective Vps4A or Vps4B mutants, HBV assembly and egress were potently blocked. PMID: 17553870
  • Inhibits Vesicular Stomatitis Virus budding but does not affect Semliki Forest Virus budding. PMID: 17913808
  • studies reveal how the VPS4 ATPases recognize their CHMP substrates to facilitate the membrane fission events required for the release of viruses, endosomal vesicles and daughter cells PMID: 17928862
  • Respiratory syncytial virus uses a Vps4-independent budding mechanism controlled by Rab11-FIP2. PMID: 18621683
  • Overall, we see no role for the ESCRT pathway in influenza virus budding and the significance of the M1-VPS28 interaction remains to be determined. PMID: 19524996
  • Both Vps4A and CHMP1A localized in the vicinity of viral cytoplasmic assembly compartments, sites of viral maturation that develop in Cytomegalovirus-infected cells. Thus, ESCRT machinery is involved in the final steps of HCMV replication. PMID: 19640981
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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