Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

E7284

Sigma-Aldrich

EPHA2 (561-end), active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

ECK

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

Pricing and availability is not currently available.

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

product line

PRECISIO® Kinase

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

74-102 nmol/min·mg

mol wt

~72 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
SRP5026E7409SRP5025
specific activity

74-102 nmol/min·mg

specific activity

24-32 nmol/min·mg

specific activity

87-120 nmol/min·mg

specific activity

27-37 nmol/min·mg

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

Gene Information

human ... EPHA2(1969)

Gene Information

human ... EPHA1(2041)

Gene Information

human ... EPHA3(2042)

Gene Information

mouse ... Epha1(13835)

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

General description

EPHA2 (ephrin receptor A2) belongs to the Eph family of receptor tyrosine kinases. It is a type I transmembrane protein, and its exoplasmic domain consists of a ligand binding domain in its N-terminal, a cysteine-rich domain, and two fibronectin type III repeats. Its cytoplasmic domain contains a juxtamembrane region, a tyrosine kinase domain, a SAM (sterile-α-motif) motif, and a PDZ-binding domain.[1]

Biochem/physiol Actions

EPHA2 binds to the ephrin-A ligand and has diverse cellular function. EPHA2 has been shown to be an oncoprotein of importance in a range of cancers. EPHA2 is overexpressed in several human cancer types and promotes malignancy through a mechanism involving RhoA-dependent destabilization of adherens junctions.[2] EPHA2 overexpression induces a FAK-dependent increase in MMP-2 expression and invasiveness and this process can be reversed by ligation of EPHA2.[3]

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.

Legal Information

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


  • Choose from one of the most recent versions:

    Certificates of Analysis (COA)

    Lot/Batch Number

    It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

    If you need assistance, please contact Customer Support

    Already Own This Product?

    Find documentation for the products that you have recently purchased in the Document Library.

    Visit the Document Library

    Blanche C Ip et al.
    Toxicological sciences : an official journal of the Society of Toxicology, 186(1), 29-42 (2021-12-23)
    Humans are consistently exposed to thousands of untested chemicals that have been detected in the follicular fluid of the ovaries, and can disrupt reproductive health. Human granulosa cells (GCs) are the functional unit of the ovarian follicle with steroidogenic and
    J C Norman et al.
    FEBS letters, 484(3), 179-183 (2000-11-18)
    Aggregation by immune complexes of receptors specific for the Fc region of IgG results in their internalisation and disposal by trafficking to lysosomes. We show here that internalisation of FcgammaRI by IFN-gamma treated U937 cells following receptor aggregation by cross-linking

    Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

    Contact Technical Service