Advanced Glycosylation End Product-Specific Receptor (AGER) (AA 23-344) (Active) protein (Fc Tag)

Details for Product No. ABIN2180572, Supplier: Log in to see
Protein Name
  • AGER
  • RAGE
  • advanced glycosylation end-product specific receptor
  • advanced glycosylation end product-specific receptor
  • AGER
  • Ager
Protein Characteristics
AA 23-344
3
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
Origin
Human
24
5
2
1
Source
HEK-293 Cells
7
6
4
4
4
2
2
1
Protein Type
Recombinant
Biological Activity
Active
Purification tag / Conjugate
Fc Tag
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Characteristics This protein carries a human IgG1 Fc tag at the C-terminus. The protein has a calculated MW of 60.8 kDa. The protein migrates as 80 - 90 kDa and 35 kDa Fc fragment under reducing (R) condition (SDS-PAGE) due to glycosylation and auto-cleavage.
Purity >60 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Biological Activity Comment Biological Activity: Measured by its binding ability in a functional ELISA. Immobilized human S100A12 at 2 μg/mL ( 100 μL/well ) can bind recombinant human AGER with a linear range of 0.032 - 20μg/mL

SDS-PAGE: due to glycosylation and auto-cleavage.
Background Advanced glycosylation end product-specific receptor (AGER) is also known as RAGE, and is a single-pass type I membrane protein which contains two Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. AGER is highly expressed in endothelial cells. AGER mediates interactions of advanced glycosylation end products (AGE), and also accumulates in vascular tissue in aging and at an accelerated rate in diabetes, as well as acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGER / RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes.
Molecular Weight 60.8 kDa
NCBI Accession NP_001127
UniProt Q15109
Research Area Neurology, Alzheimer's Disease
Pathways Carbohydrate Homeostasis, Toll-Like Receptors Cascades, Smooth Muscle Cell Migration
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Advanced Glycosylation End Product-Specific Receptor (AGER) (AA 23-344) (Active) protein (Fc Tag) (ABIN2180572) Human RAGE, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained over...
Background publications Xue, Rai, Singer, Chabierski, Xie, Reverdatto, Burz, Schmidt, Hoffmann, Shekhtman: "Advanced glycation end product recognition by the receptor for AGEs." in: Structure (London, England : 1993), Vol. 19, Issue 5, pp. 722-32, 2011 (PubMed).

Jin, Chen, Luo, Ding, Liu: "S100A14 stimulates cell proliferation and induces cell apoptosis at different concentrations via receptor for advanced glycation end products (RAGE)." in: PLoS ONE, Vol. 6, Issue 4, pp. e19375, 2011 (PubMed).

Fang, Lue, Yan, Xu, Luddy, Chen, Walker, Stern, Yan, Schmidt, Chen, Yan: "RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning/memory in a mouse model of Alzheimer's disease." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 24, Issue 4, pp. 1043-55, 2010 (PubMed).

Did you look for something else?