- PA5-28553 - Invitrogen Antibodies VPS35L antibody

Submitted references Human Papillomavirus 16 L2 Recruits both Retromer and Retriever Complexes during Retrograde Trafficking of the Viral Genome to the Cell Nucleus.

Pim D, Broniarczyk J, Siddiqa A, Massimi P, Banks L
Journal of virology 2021 Jan 13;95(3)

Regulation of murine copper homeostasis by members of the COMMD protein family.

Singla A, Chen Q, Suzuki K, Song J, Fedoseienko A, Wijers M, Lopez A, Billadeau DD, van de Sluis B, Burstein E
Disease models & mechanisms 2021 Jan 1;14(1)

Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting.

Evans AJ, Daly JL, Anuar ANK, Simonetti B, Cullen PJ
Journal of cell science 2020 Aug 3;133(15)

COMMD10-Guided Phagolysosomal Maturation Promotes Clearance of Staphylococcus aureus in Macrophages.

Ben Shlomo S, Mouhadeb O, Cohen K, Varol C, Gluck N
iScience 2019 Apr 26;14:147-163

Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling.

McNally KE, Faulkner R, Steinberg F, Gallon M, Ghai R, Pim D, Langton P, Pearson N, Danson CM, Nägele H, Morris LL, Singla A, Overlee BL, Heesom KJ, Sessions R, Banks L, Collins BM, Berger I, Billadeau DD, Burstein E, Cullen PJ
Nature cell biology 2017 Oct;19(10):1214-1225

COMMD1 is linked to the WASH complex and regulates endosomal trafficking of the copper transporter ATP7A.

Phillips-Krawczak CA, Singla A, Starokadomskyy P, Deng Z, Osborne DG, Li H, Dick CJ, Gomez TS, Koenecke M, Zhang JS, Dai H, Sifuentes-Dominguez LF, Geng LN, Kaufmann SH, Hein MY, Wallis M, McGaughran J, Gecz J, Sluis Bv, Billadeau DD, Burstein E
Molecular biology of the cell 2015 Jan 1;26(1):91-103

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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Fig. 1. COMMD protein deficiency causes the destabilization of the CCC complex in enterocytes and hepatocytes. (A) Expression of CCC complex subunits was examined by immunoblotting in enterocytes isolated from intestinal-specific Commd1 and Commd9 knockout mice ( Commd1 DeltaIEC and Commd9 DeltaIEC , respectively). Animals carrying the floxed alleles served as controls ( Commd1 fl/fl and Commd9 fl/fl , respectively). beta-Actin served as a loading control. (B) Same as in A, but using liver lysates from hepatocyte-specific COMMD-deficient mice ( Commd1 DeltaHEP , Commd6 DeltaHEP and Commd9 DeltaHEP ) and corresponding controls. Arrowheads indicate the band specific to the antibody.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: FIGURE 3: Interaction and colocalization of the CCC and WASH complexes. (A) Interaction map between CCC complex components and other cellular complexes were drawn using data extracted from NCBI. Intracomplex interactions, where useful, are also indicated. Human studies are depicted, and interactions identified in this study are depicted in red. (B) Coimmunoprecipitation of endogenous CCC subunits (CCDC22, CCDC93, and C16orf62) with the WASH components (FAM21 and WASH) was noted using HeLa cell lysates. (C) Colocalization of endogenous COMMD1 (green) and CCDC93 (red) or C16orf62 (red) was examined by immunostaining in HeLa cells. Scale bar, 5 mum. (D) Colocalization of endogenous COMMD1 (green) with WASH (red, top), and the retromer subunit VPS35 (red, bottom) was examined by immunofluorescence staining of HeLa cells. Scale bar, 5 mum.

PA5-28553

Antibody data