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AGER / RAGE Protein (His Tag) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
11629-H08H
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Protein Production & Purification Service

Advanced glycosylation end product-specific receptor Protein Datasheet

 

AGER / RAGE Protein Price Inquiry ( Available Sizes )

AGER / RAGE Protein Product Information

Synonym : AGER
Protein Construction:

A DNA sequence encoding the mature form of  human AGER (NP_001127) extracellular domain (Met1-Ala 344) was expressed and purified.

Source: Human
Expression Host: Human Cells

AGER / RAGE Protein QC Testing

Purity: > 78 % as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

AGER / RAGE protein

Bio-activity:

1. Measured by its binding ability in a functional ELISA.
2. Immobilized recombinant human AGER-His (Cat:11629-H08H) at 10 μg/mL (100 μl/well) can bind biotinylated mouse His-S100A1 (Cat:50266-M07E) with a linear range of 15.6-250 ng/mL.
3. Measured by its ability to bind biotinylated human S100A1 (Cat:10179-HNAE) in functional ELISA.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability: Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal: Ala 23
Molecular Mass:

The recombinant human AGER consists of  322 amino acids and predicts a molecular mass of 34.2 KDa. It migrates as an approximately 48 KDa band in SDS-PAGE under reducing conditions.

Formulation: Lyophilized from sterile PBS, pH 7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

AGER / RAGE Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

AGER / RAGE Protein Related Products & Topics

Related Areas:

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
RAGE/AGER Human RAGE/AGER/Fc Protein, Recombinant 11629-H02H
RAGE/AGER Human AGER / RAGE Protein, Recombinant 11629-H08H
RAGE/AGER Human AGER / RAGE Protein, Recombinant 11629-HNCH
RAGE/AGER Mouse RAGE/AGER Protein, Recombinant 50489-M08H

Antibodies:

Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
Mouse
RAGE/AGER
WB, ELISA RAGE/AGER Antibody, Rabbit PAb 50489-RP01
Mouse
RAGE/AGER
WB, ELISA RAGE/AGER Antibody, Rabbit PAb (Antigen Affinity Purified) 50489-RP02

AGER / RAGE Protein Description

Advanced glycosylation end product-specific receptor, also known as receptor for advanced glycosylation end products, AGER and RAGE, is a single-pass type I membrane protein. AGER / RAGE contains two Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. AGER / RAGE mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. AGER / RAGE acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE / RAGE signaling plays an important role in regulating the production / expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction between AGER / RAGE and S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction between AGER / RAGE and S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. AGER / RAGE contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons.

References

  1. Sugaya K. et al., 1994, Genomics. 23: 408-19.
  2. Neeper M. et al., 1992, J Biol Chem. 267: 14998-5004.
  3. Xie T. et al., 2003, Genome Res. 13: 2621-36.
  4. Moroz OV. et al., 2009, BMC Biochem. 10: 11.
  5. Fang F. et al., 2010, FASEB J. 24: 1043-55.