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AB69507

Anti-SHARPIN antibody

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(8 Publications)

Mouse Polyclonal SHARPIN antibody. Carrier free. Suitable for WB and reacts with Human samples. Cited in 8 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human SHARPIN.

View Alternative Names

SIPL1, PSEC0216, SHARPIN, Sharpin, Shank-associated RH domain-interacting protein, Shank-interacting protein-like 1, hSIPL1

2 Images
Western blot - Anti-SHARPIN antibody (AB69507)
  • WB

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Western blot - Anti-SHARPIN antibody (AB69507)

All lanes:

Western blot - Anti-SHARPIN antibody (ab69507) at 1/500 dilution

Lane 1:

SHARPIN transfected 293T cell lysate at 25 µg

Lane 2:

Non-transfected 293T cell lysate at 25 µg

Secondary

All lanes:

Goat Anti-Mouse IgG (H&L)-HRP Conjugate at 1/2500 dilution

Predicted band size: 40 kDa

Observed band size: 36 kDa

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Western blot - Anti-SHARPIN antibody (AB69507)
  • WB

CiteAb

Western blot - Anti-SHARPIN antibody (AB69507)

SHARPIN western blot using anti-SHARPIN antibody ab69507. Publication image and figure legend from de Franceschi, N., Peuhu, E., et al., 2015, PLoS One, PubMed 26600301.

ab69507 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab69507 please see the product overview.

Fine mapping of the RNF31 binding site in SHARPIN.(A) Western blot analysis of SHARPIN and β-tubulin levels in control- or SHARPIN-silenced PC3 cells. (B) TNF-induced NF-κB promoter activity of SHARPIN- or control-silenced PC3 cells was measured using a luciferase reporter assay. (n = 3 with 5 replicates each). (C) TNF-induced NF-κB promoter activity of SHARPIN-silenced PC3 cells, expressing GFP alone, WT or mutant GFP-SHARPIN (n = 6–15 measurements from 2–3 experiments). (D,E) Interaction between RNF31 and WT or mutant GST-SHARPIN was determined using an ELISA-based binding assay (n = 3) (D) or Far-Western analysis (E). All numerical data are mean ± s.e.m. *** : p<0.001, ** : p<0.01, * : p<0.05.

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Key facts

Host species

Mouse

Clonality

Polyclonal

Isotype

IgG

Carrier free

Yes

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human SHARPIN.

Q9H0F6

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/1000", "WB-species-notes": "<p>(predicted molecular weight: Isoform 2, 34 kDa; Isoform 1, 40 kDa).</p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: 100% PBS
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
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Supplementary information

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

SHARPIN also known as SHANK-associated RH domain-interacting protein is a multi-functional protein with a molecular mass of approximately 34 kDa. It primarily acts as a ubiquitin-binding protein and is a part of the LUBAC (Linear Ubiquitin Chain Assembly Complex) involved in various cellular signaling pathways. SHARPIN is expressed in a range of tissues but is highly abundant in lymphoid tissues and the brain. Its mechanical actions involve binding and modulating ubiquitin chains which plays a role in regulating protein stability and signaling processes in cells.
Biological function summary

SHARPIN engages in significant cellular functions by being a critical component of the LUBAC complex. This complex is central to the activation of NF-kB signaling by mediating linear ubiquitination of specific substrate proteins influencing inflammatory responses and cell death regulation. In the immune system SHARPIN regulates the TNF receptor signaling and helps maintain homeostasis. Its absence or mutation can lead to dysregulated cell survival and immune responses highlighting its importance in maintaining cellular functions.

Pathways

SHARPIN integrates into the NF-kB and Wnt signaling pathways which are vital for regulating immune responses and cell fate decisions. Within the NF-kB pathway SHARPIN cooperates with other LUBAC components such as HOIP and HOIL-1L to facilitate ubiquitination necessary for pathway activation. Additionally SHARPIN influences the Wnt pathway through interactions with Dishevelled proteins contributing to developmental and stem cell signaling. The coordination of these pathways by SHARPIN highlights its role in cellular communication and signaling.

SHARPIN has connections to conditions such as chronic inflammation and immunodeficiency syndromes. Dysregulation in SHARPIN function can contribute to chronic inflammatory diseases including psoriasis due to improper NF-kB pathway regulation. Its association with HOIP and HOIL-1L through the LUBAC complex also links it to autoinflammatory conditions characterized by immune system imbalances. SHARPIN mutations are implicated in skin and immune disorders reflecting its broad impact on health and disease manifestation.
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Product protocols

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

Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed : 21455173, PubMed : 21455180, PubMed : 21455181). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed : 21455173, PubMed : 21455180, PubMed : 21455181). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed : 21455173, PubMed : 21455180, PubMed : 21455181). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed : 21455173, PubMed : 21455180, PubMed : 21455181). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed : 28481331). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed : 28481331). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed : 28481331). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed : 23708998).
See full target information SHARPIN
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Publications (8)

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

Cell communication and signaling : CCS 17:101 PubMed31429758

2019

Sharpin suppresses β1-integrin activation by complexing with the β1 tail and kindlin-1.

Applications

Unspecified application

Species

Unspecified reactive species

Juan Gao,Yun Bao,Shushu Ge,Peisen Sun,Jiaojiao Sun,Jianmin Liu,Feng Chen,Li Han,Zhongyuan Cao,Jun Qin,Gilbert C White,Zhen Xu,Yan-Qing Ma

BioResearch open access 7:81-89 PubMed29862142

2018

LUBAC and ABIN-1 Modulate TRAIL-Based NF-κB Induction in Human Embryonic Kidney 293 Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Sebastian Dorn,Christian Schoergenhofer,Michael Krainer,Markus Müller,Bernd Jilma

Oncotarget 8:77137-77151 PubMed29100376

2017

SHARPIN stabilizes estrogen receptor α and promotes breast cancer cell proliferation.

Applications

Unspecified application

Species

Unspecified reactive species

Ting Zhuang,Sifan Yu,Lichen Zhang,Huijie Yang,Xin Li,Yingxiang Hou,Zhenhua Liu,Yuanyuan Shi,Weilong Wang,Na Yu,Anqi Li,Xuefeng Li,Xiumin Li,Gang Niu,Juntao Xu,Muhammad Sharif Hasni,Kun Mu,Hui Wang,Jian Zhu

Journal of cell science 130:3094-3107 PubMed28775156

2017

The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex.

Applications

Unspecified application

Species

Unspecified reactive species

Meraj H Khan,Siiri I Salomaa,Guillaume Jacquemet,Umar Butt,Mitro Miihkinen,Takahiro Deguchi,Elena Kremneva,Pekka Lappalainen,Martin J Humphries,Jeroen Pouwels

Neoplasia (New York, N.Y.) 19:84-92 PubMed28063307

2017

SHARPIN Facilitates p53 Degradation in Breast Cancer Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Huijie Yang,Sifan Yu,Weilong Wang,Xin Li,Yingxiang Hou,Zhenhua Liu,Yuanyuan Shi,Kun Mu,Gang Niu,Juntao Xu,Hui Wang,Jian Zhu,Ting Zhuang

PloS one 10:e0143423 PubMed26600301

2015

Mutually Exclusive Roles of SHARPIN in Integrin Inactivation and NF-κB Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Nicola De Franceschi,Emilia Peuhu,Maddy Parsons,Sami Rissanen,Ilpo Vattulainen,Marko Salmi,Johanna Ivaska,Jeroen Pouwels

The EMBO journal 31:3845-55 PubMed23032186

2012

A20 inhibits LUBAC-mediated NF-κB activation by binding linear polyubiquitin chains via its zinc finger 7.

Applications

Unspecified application

Species

Unspecified reactive species

Kelly Verhelst,Isabelle Carpentier,Marja Kreike,Laura Meloni,Lynn Verstrepen,Tobias Kensche,Ivan Dikic,Rudi Beyaert

Nature cell biology 13:1315-24 PubMed21947080

2011

SHARPIN is an endogenous inhibitor of β1-integrin activation.

Applications

Unspecified application

Species

Unspecified reactive species

Juha K Rantala,Jeroen Pouwels,Teijo Pellinen,Stefan Veltel,Petra Laasola,Elina Mattila,Christopher S Potter,Ted Duffy,John P Sundberg,Olli Kallioniemi,Janet A Askari,Martin J Humphries,Maddy Parsons,Marko Salmi,Johanna Ivaska
View all publications
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