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SAB4200646

Sigma-Aldrich

Monoclonal Anti-ALIX/PDCD6IP antibody produced in mouse

clone ALIX-1, purified from hybridoma cell culture

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

ALIX-1, monoclonal

form

buffered aqueous solution

species reactivity

human

concentration

~1 mg/mL

technique(s)

flow cytometry: 5-10 μg/test using using human MOLT4 cells
immunoblotting: 2-5 μg/mL using using whole extracts of human MOLT4 cells.
immunofluorescence: 10-20 μg/mL using using human HeLa cells
immunoprecipitation (IP): 10-20 μg/mL using using lysates of human MOLT4 cells.

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PDCD6IP(10015)

General description

Anti-ALIX/PDCD6IP antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma ALIX-1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a peptide corresponding to an internal region of human ALIX/ PDCD6IP, conjugated to KLH. ALIX (Apoptosis-linked gene 2 (ALG-2)-interacting protein X), also named Programmed Cell Death 6 interacting protein (PDCD6IP).

Immunogen

peptide corresponding to an internal region of human ALIX/ PDCD6IP

Application

Monoclonal Anti-ALIX/PDCD6IP antibody has been used in
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence
  • flow cytometry

Biochem/physiol Actions

ALIX (Apoptosis-linked gene 2 (ALG-2)-interacting protein X) plays a role in ESCRT (endosomal sorting complexes required for transport) pathway. It is involved in the abscission stage of cytokinesis, in intralumenal endosomal localization, and in enveloped virus budding. Overexpression of this protein can block apoptosis. In addition, ALIX binds to PDCD6, a protein required for apoptosis, in a calcium-dependent manner. ALIX also binds to endophilins, proteins that regulate membrane shape during endocytosis. Overexpression of ALIX and endophilins results in cytoplasmic vacuolization, which may be partly responsible for the protection against cell death.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
Morita E, et al.
The Embo Journal, 26(19), 4215-4227 (2007)
AIP1/Alix is a binding partner of Sendai virus C protein and facilitates virus budding
Sakaguchi T, et al.
Journal of Virology, 79(14), 8933-8941 (2005)
The multiple personalities of Alix
Odorizzi G.
Journal of Cell Science, 119(15), 3025-3032 (2006)
Christine Chatellard-Causse et al.
The Journal of biological chemistry, 277(32), 29108-29115 (2002-05-30)
ALG-2-interacting protein X (Alix), also known as AIP1, is a cytoplasmic protein ubiquitously expressed and concentrated in phagosomes and exosomes. Alix may regulate apoptosis since it binds apoptosis-linked gene 2 (ALG-2), a Ca2+-binding protein necessary for cell death, and also
Xuefeng Ren et al.
Traffic (Copenhagen, Denmark), 12(10), 1282-1290 (2011-04-27)
Most membrane-enveloped viruses bud from infected cells by hijacking the host ESCRT machinery. The ESCRTs are recruited to the budding sites by viral proteins that contain short proline (Pro)-rich motifs (PRMs) known as late domains. The late domains probably evolved

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