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AB114898

Recombinant Human Ephrin A2 protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human Ephrin A2 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 213 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

EPLG6, LERK6, EFNA2, Ephrin-A2, EPH-related receptor tyrosine kinase ligand 6, HEK7 ligand, LERK-6, HEK7-L

1 Images
SDS-PAGE - Recombinant Human Ephrin A2 protein (GST tag N-Terminus) (AB114898)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Ephrin A2 protein (GST tag N-Terminus) (AB114898)

12.5% SDS-PAGE showing ab114898 at approximately 50.43kDa.
Stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB, SDS-PAGE

applications

Biologically active

No

Accession

O43921

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

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>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Recombinant protein</p>" } } }

Sequence info

[{"sequence":"MAPAQRPLLPLLLLLLPLPPPPFARAEDAARANSDRYAVYWNRSNPRFHAGAGDDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMEHYVLYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNAVDRPCLRLKVYVRPTNETLYEAPEPIFTSNNSCSSPGGCRLFLSTIPVLWTLLGS","proteinLength":"Full Length","predictedMolecularWeight":"50.43 kDa","actualMolecularWeight":null,"aminoAcidEnd":213,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"O43921","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°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.

Ephrin A2 also known as EFNA2 is a member of the ephrin family which plays an important role in cellular processes. This protein is a glycosylphosphatidylinositol (GPI)-anchored ligand for Eph receptors which are a type of receptor tyrosine kinases. Ephrin A2 has a mass of approximately 25 kDa. It is mostly expressed in the nervous system as well as in the endothelial cells of blood vessels. Ephrin A2 is important for mediating cell signaling that affects morphology and cellular movement.
Biological function summary

Ephrin A2 is involved in cell positioning and boundary formation. It is essential during embryonic development for tissue patterning. The ephrin A2 binds to Eph receptors often forming a complex that triggers bidirectional signaling. This complex affects neuronal growth cones guiding axon pathfinding and is significant in neurogenesis. Its signaling impacts cellular adhesion and repulsion which regulates how cells interact with their surroundings and other cells.

Pathways

Ephrin A2 is integrated into the Eph/ephrin signaling pathway which is important for various cellular responses. This signaling impacts the Rho family of GTPases which play a role in mediating cytoskeletal dynamics. Ephrin A2 also interacts with the MAPK/ERK pathway contributing to the regulation of cell proliferation and differentiation. Within these pathways it associates with proteins like EphA4 and ephrin A5 influencing pathway outcomes.

Ephrin A2 has associations with cancer particularly in tumor growth and angiogenesis. Altered Ephrin A2 signaling can contribute to the progression of cancers by affecting vascularization and cell migration. Additionally its dysregulation is linked to neurodegenerative conditions such as Alzheimer's disease. Through these diseases Ephrin A2 interacts with various proteins including amyloid precursor protein and tau which are involved in disease pathologies.

Specifications

Form

Liquid

General info

Function

Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity).

Sequence similarities

Belongs to the ephrin family.

Product protocols

Target data

Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. With the EPHA2 receptor may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity).
See full target information EFNA2

Publications (1)

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

Frontiers in immunology 12:793517 PubMed34975898

2021

The Expression of ephrinA1/ephA2 Receptor Increases in Chronic Rhinosinusitis and ephrinA1/ephA2 Signaling Affects Rhinovirus-Induced Innate Immunity in Human Sinonasal Epithelial Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Sang Hag Lee,Sung Hoon Kang,Mun Soo Han,Ji Won Kwak,Hyeon Geun Kim,Tae Hoon Lee,Da Bin Lee,Tae Hoon Kim
View all publications

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