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AB127584

Recombinant Human EGFL6 protein

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(1 Publication)

Recombinant Human EGFL6 protein is a Human Fragment protein, in the 30 to 219 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.

View Alternative Names

MAEG, PP648, UNQ281/PRO320, EGFL6, Epidermal growth factor-like protein 6, EGF-like protein 6, MAM and EGF domains-containing gene protein

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His-DHFR tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q8IUX8

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

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":"20.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":219,"aminoAcidStart":30,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q8IUX8","tags":[{"tag":"His-DHFR","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
False

Supplementary information

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

EGFL6 also known as Epidermal Growth Factor-Like Protein 6 or MAEG is a secreted protein that plays a role in the regulation of cell growth. It belongs to the epidermal growth factor (EGF) repeat superfamily and has an approximate mass of 70 kDa. EGFL6 is expressed in various tissues with higher expression noted in fetal tissues particularly the lung and kidney as well as in certain adult tissues like the ovary.
Biological function summary

This protein influences cell proliferation and differentiation. EGFL6 is not a part of a larger protein complex but functions through its interactions with other cellular components. Its activity affects cell behavior which is especially noted during development and tissue regeneration processes. EGFL6 modulates the extracellular environment through binding to receptor tyrosine kinases mediating signaling that promotes cellular motility and survival.

Pathways

EGFL6 integrates into significant pathways such as the PI3K/AKT and MAPK signaling pathways. Through these pathways it maintains cellular processes related to growth and survival by interacting with proteins like AKT1 and MAPK1. These signaling cascades are fundamental in mediating responses to growth factors and adjusting cell fate decisions.

Aberrant expression of EGFL6 associates with conditions such as cancer specifically ovarian cancer and melanoma. In these contexts EGFL6 interplays with proteins like VEGF contributing to tumor growth and angiogenesis. Its role in disease suggests potential as a therapeutic target for interventions designed to modulate cancer progression.

Specifications

Form

Lyophilized

Additional notes

Purified via His tag

General info

Function

May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly (By similarity).

Sequence similarities

Belongs to the nephronectin family.

Product protocols

Target data

May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly (By similarity).
See full target information EGFL6

Publications (1)

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

Arthritis research & therapy 15:R165 PubMed24286167

2013

Decreased expression of the endothelial cell-derived factor EGFL7 in systemic sclerosis: potential contribution to impaired angiogenesis and vasculogenesis.

Applications

sELISA

Species

Unspecified reactive species

Mirko Manetti,Serena Guiducci,Eloisa Romano,Jérôme Avouac,Irene Rosa,Barbara Ruiz,Gemma Lepri,Silvia Bellando-Randone,Lidia Ibba-Manneschi,Yannick Allanore,Marco Matucci-Cerinic
View all publications

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