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SAB4200025

Sigma-Aldrich

Anti-VPS4 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-Vacuolar protein sorting 4

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200 μL
513,00 €

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200 μL
513,00 €

About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

513,00 €


Per informazioni sulla disponibilità, contatta il Servizio Clienti.

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Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen ~50 kDa

Reattività contro le specie

rat, human, mouse

Concentrazione

~1.0 mg/mL

tecniche

immunoprecipitation (IP): 2-4 μg using lysates of human HeLa cells
western blot: 1-2 μg/mL using whole extracts of mouse 3T3 or rat NRK cells

N° accesso UniProt

applicazioni

research pathology

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... VPS4A(27183)
mouse ... Vps4a(116733)
rat ... Vps4a(246772)

Descrizione generale

Vacuolar protein sorting-associated protein 4 (Vps4) is a member of the AAA protein family (ATPases associated with diverse cellular activities). Vps4 exists as two orthologs in humans (VPS4A and VPS4B). The gene encoding Vps4A is mapped to chromosome 16q22, while the gene for Vps4B resides on chromosome 18q21-q22.

Specificità

Anti-VPS4 recognizes human, mouse, and rat VPS4A and VPS4B.

Applicazioni

Anti-VPS4 antibody has been used in
  • immunoprecipitation
  • immunofluorescence Confocal Microscopy
  • immunohistochemistry
  • western blotting

Azioni biochim/fisiol

Vacuolar protein sorting-associated protein 4 (VPS4) mediates endosomal membrane protein sorting, retroviral budding and cytokinesis by recognizing membrane-associated ESCRT-III assemblies and catalyzing their disassembly.

Stato fisico

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Stoccaggio e stabilità

Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Aiqin Hu et al.
BMC genetics, 20(1), 7-7 (2019-01-13)
Vacuolar protein sorting-associated protein 4B (VPS4B) is a member of the ATP enzyme AAA protein family, and is mainly involved in protein degradation and cell membrane fusion. Recently, a dominant mutation in this gene was identified in human dentin dysplasia
Shimon Harel et al.
Biophysical journal, 121(21), 4229-4238 (2022-09-01)
The assembly and budding of newly formed human immunodeficiency virus-1 (HIV-1) particles occur at the plasma membrane of infected cells. Although the molecular basis for viral budding has been studied extensively, investigation of its spatiotemporal characteristics has been limited by
The AAA-ATPase VPS4 regulates extracellular secretion and lysosomal targeting of alpha-synuclein
Hasegawa T, et al.
PLoS ONE, 6(12), e29460-e29460 (2011)
ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4
Thoresen SB, et al.
Nature Cell Biology, 16(6), 550-560 (2014)
Takafumi Hasegawa et al.
PloS one, 6(12), e29460-e29460 (2012-01-05)
Many neurodegenerative diseases share a common pathological feature: the deposition of amyloid-like fibrils composed of misfolded proteins. Emerging evidence suggests that these proteins may spread from cell-to-cell and encourage the propagation of neurodegeneration in a prion-like manner. Here, we demonstrated

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