JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB82822

Recombinant Human ADAM10 protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human ADAM10 protein is a Human Fragment protein, in the 214 to 672 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

CD156c, KUZ, MADM, ADAM10, Disintegrin and metalloproteinase domain-containing protein 10, ADAM 10, CDw156, Kuzbanian protein homolog, Mammalian disintegrin-metalloprotease

1 Images
SDS-PAGE - Recombinant Human ADAM10 protein (AB82822)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ADAM10 protein (AB82822)

ab82822 on SDS-PAGE.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

6x His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O14672

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 Constituents: PBS, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":672,"aminoAcidStart":214,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O14672","tags":[{"tag":"6x His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The ADAM10 protein also known as CD156c is a member of the ADAM (a disintegrin and metalloprotease) family. It functions as a metalloproteinase enzyme involved in the ectodomain shedding of various cell surface proteins. ADAM10 has an approximate molecular weight of 85 kDa. This protein has broad expression in various tissues including the brain heart and liver and performs key enzymatic activities that affect cellular communication.
Biological function summary

ADAM10 contributes to development and regulation of synapses in the central nervous system being part of the membrane protein complex. It processes amyloid precursor protein (APP) and other substrates excising their extracellular domains and influencing cell signaling pathways. ADAM10 activity regulates Notch signaling a mechanism essential for cell differentiation and tissue homeostasis.

Pathways

ADAM10 activity intersects with several important biological processes including the Notch and Epidermal Growth Factor Receptor (EGFR) pathways. Notch signaling pathway involves interactions with ligands like Jagged and Delta impacting cell fate decisions. In the EGFR pathway ADAM10 regulates the availability of ligands such as EGF affecting the receptor’s signaling cascades related to cell proliferation and survival.

ADAM10 dysregulation associates with Alzheimer’s disease and cancer. ADAM10's role in cleaving APP is linked to Alzheimer's where altered activity may affect amyloid-beta production and plaque formation. In cancer ADAM10 modulates cell adhesion and migration influencing tumor progression and metastasis. ADAM10 interactions with proteins in these contexts such as β-Catenin in cancer illustrate its impact on pathophysiological processes.

Specifications

Form

Liquid

General info

Function

Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed : 11786905, PubMed : 12475894, PubMed : 20592283, PubMed : 24990881, PubMed : 26686862, PubMed : 28600292, PubMed : 31792032). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed : 26686862, PubMed : 28600292, PubMed : 31792032, PubMed : 34739841, PubMed : 37516108). Cleaves the membrane-bound precursor of TNF at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed : 20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed : 11786905, PubMed : 26686862, PubMed : 29224781, PubMed : 34739841). Contributes to the normal cleavage of the cellular prion protein (PubMed : 11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed : 12475894). Also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Required for the development of type 1 transitional B cells into marginal zone B cells, probably by cleaving Notch (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed : 17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed : 19114711, PubMed : 21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed : 26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed : 24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed : 16239146). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE-cadherin/CDH5 in endothelial cells (PubMed : 28600292).. (Microbial infection) Promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting formation of toxin pores.

Post-translational modifications

The precursor is cleaved by furin and PCSK7.

Product protocols

Target data

Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed : 11786905, PubMed : 12475894, PubMed : 20592283, PubMed : 24990881, PubMed : 26686862, PubMed : 28600292, PubMed : 31792032). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed : 26686862, PubMed : 28600292, PubMed : 31792032, PubMed : 34739841, PubMed : 37516108). Cleaves the membrane-bound precursor of TNF at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed : 20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed : 11786905, PubMed : 26686862, PubMed : 29224781, PubMed : 34739841). Contributes to the normal cleavage of the cellular prion protein (PubMed : 11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed : 12475894). Also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Required for the development of type 1 transitional B cells into marginal zone B cells, probably by cleaving Notch (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed : 17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed : 19114711, PubMed : 21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed : 26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed : 24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed : 16239146). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE-cadherin/CDH5 in endothelial cells (PubMed : 28600292).. (Microbial infection) Promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting formation of toxin pores.
See full target information ADAM10

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com