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AB97889

Anti-C16orf62 antibody

4

(1 Review)

|

(7 Publications)

Rabbit Polyclonal C16orf62 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 7 publications. Immunogen corresponding to Recombinant Fragment Protein within Human VPS35L aa 1 to C-terminus.

View Alternative Names

C16orf62, 101F10.2, VPS35L, VPS35 endosomal protein-sorting factor-like, Esophageal cancer-associated protein

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-C16orf62 antibody (AB97889)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-C16orf62 antibody (AB97889)

ab97889, at 1/500 dilution, staining C16orf62 by immunohistochemistry (parafin embedded sections), in Cal27 xenograft.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Recombinant Fragment Protein within Human VPS35L aa 1 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q7Z3J2

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

C16orf62 also known as Chromosome 16 Open Reading Frame 62 is a lesser-known but important protein with a predicted mass of approximately 40 kDa. These proteins are most notably expressed in tissues such as the pancreas and liver. While not widely studied it is thought that C16orf62 might contribute to processes that have not been fully elucidated yet. As research on this gene progresses a clearer understanding of its precise mechanical roles will likely emerge.
Biological function summary

C16orf62 plays an important role in cellular homeostasis and metabolic regulation. It is part of a multiprotein complex called the ER-associated degradation (ERAD) complex. Within this complex C16orf62 contributes to the detection and degradation of misfolded proteins maintaining protein quality control inside the cells. The balance achieved by C16orf62 and its complex partners is critical in preventing the accumulation of defective proteins that can lead to cellular stress and dysfunction.

Pathways

C16orf62's function as part of the ERAD complex integrates into the broader protein processing pathways in the endoplasmic reticulum. This regulation involves pathways like the ER stress response and the ubiquitin-proteasome system. C16orf62 collaborates with other proteins in these pathways such as ubiquitin ligases which tag misfolded proteins for degradation. These interactions emphasize its role in maintaining cellular protein homeostasis and adapting to stress conditions.

The misregulation of C16orf62 has implications for conditions like cystic fibrosis and certain liver diseases. In cystic fibrosis the improper degradation of misfolded proteins can exacerbate the disease pathogenesis. This protein functioning with partners like the CFTR protein highlights its potential connection to the disease mechanisms. Similarly in liver disorders defects in protein quality control pathways can lead to accumulation of toxic proteins contributing to disease progression. Understanding C16orf62's influence on these disorders could open new avenues for therapeutic approaches.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Acts as a component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5 : ITGB1) (PubMed : 28892079). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes (PubMed : 28892079). In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling (PubMed : 28892079). Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association with the CCC complex and cooperation with the WASH complex on early endosomes. Does not seem to be required for CCC complex stability (PubMed : 25355947).. (Microbial infection) The heterotrimeric retriever complex, in collaboration with the CCC complex, mediates the exit of human papillomavirus to the cell surface.
See full target information VPS35L

Publications (7)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 16:8794 PubMed41038817

2025

Identification of a RAB32-LRMDA-Commander membrane trafficking complex reveals the molecular mechanism of human oculocutaneous albinism type 7.

Applications

Unspecified application

Species

Unspecified reactive species

Rebeka Butkovič,Michael D Healy,Cecilia de Heus,Alexander P Walker,Wyatt Beyers,Kerrie E McNally,Philip A Lewis,Kate J Heesom,Nalan Liv,Judith Klumperman,Santiago Di Pietro,Brett M Collins,Peter J Cullen

Nature communications 16:6990 PubMed40738907

2025

Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation.

Applications

Unspecified application

Species

Unspecified reactive species

Carlos Antón-Plágaro,Kai-En Chen,Qian Guo,Meihan Liu,Ashley J Evans,Philip A Lewis,Kate J Heesom,Kevin A Wilkinson,Brett M Collins,Peter J Cullen

Proceedings of the National Academy of Sciences of the United States of America 122:e2501111122 PubMed40587794

2025

Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.

Applications

Unspecified application

Species

Unspecified reactive species

James L Daly,Kai-En Chen,Rebeka Butkovič,Qian Guo,Michael D Healy,Eva Pennink,Georgia Gamble-Strutt,Zara Higham,Edmund R R Moody,Philip A Lewis,Kate J Heesom,Tom A Williams,Kirsty J McMillan,Brett M Collins,Peter J Cullen

Nature communications 15:7180 PubMed39168982

2024

Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Rebeka Butkovič,Alexander P Walker,Michael D Healy,Kerrie E McNally,Meihan Liu,Tineke Veenendaal,Kohji Kato,Nalan Liv,Judith Klumperman,Brett M Collins,Peter J Cullen

Cell 186:2219-2237.e29 PubMed37172566

2023

Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Michael D Healy,Kerrie E McNally,Rebeka Butkovič,Molly Chilton,Kohji Kato,Joanna Sacharz,Calum McConville,Edmund R R Moody,Shrestha Shaw,Vicente J Planelles-Herrero,Sathish K N Yadav,Jennifer Ross,Ufuk Borucu,Catherine S Palmer,Kai-En Chen,Tristan I Croll,Ryan J Hall,Nikeisha J Caruana,Rajesh Ghai,Thi H D Nguyen,Kate J Heesom,Shinji Saitoh,Imre Berger,Christiane Schaffitzel,Tom A Williams,David A Stroud,Emmanuel Derivery,Brett M Collins,Peter J Cullen

Journal of medical genetics : PubMed36113987

2022

Clinical diversity and molecular mechanism of VPS35L-associated Ritscher-Schinzel syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Shiomi Otsuji,Yosuke Nishio,Maki Tsujita,Marlene Rio,Céline Huber,Carlos Antón-Plágaro,Seiji Mizuno,Yoshihiko Kawano,Satoko Miyatake,Marleen Simon,Ellen van Binsbergen,Richard H van Jaarsveld,Naomichi Matsumoto,Valerie Cormier-Daire,Peter J Cullen,Shinji Saitoh,Kohji Kato

Nature cell biology 19:1214-1225 PubMed28892079

2017

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

Applications

WB

Species

Unspecified reactive species

Kerrie E McNally,Rebecca Faulkner,Florian Steinberg,Matthew Gallon,Rajesh Ghai,David Pim,Paul Langton,Neil Pearson,Chris M Danson,Heike Nägele,Lindsey L Morris,Amika Singla,Brittany L Overlee,Kate J Heesom,Richard Sessions,Lawrence Banks,Brett M Collins,Imre Berger,Daniel D Billadeau,Ezra Burstein,Peter J Cullen
View all publications

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