0 products, total $0.+86-400-890-9989      Login |  Register 中文한국어

Browse By Molecule:

Your Position: Home > Recombinant Protein > Human Cell Expressed > AGER / RAGE Protein

AGER / RAGE Protein PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
11629-HCCH
  YES          

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_001127.1) (Met1-Ala 344) was expressed with six amino acids (LEVLFQ) at the C- terminus.

Source: Human
Expression Host: Human Cells

AGER / RAGE Protein QC Testing

Purity: > 95 % as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

AGER / RAGE protein

Bio-activity:

1. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human Fc-S100B (Cat:10181-H01H) in a functional ELISA.
2. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant mouse S100B-Fc (Cat:50986-M01H) in a functional ELISA.
3. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human S100A1-Fc (Cat:10179-H01HE) in a functional ELISA.
4. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human APP-Fc (Cat:10703-H02H) in a 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  329 amino acids and predicts a molecular mass of 35 KDa. It migrates as an approximately 46-52 KDa band in SDS-PAGE under reducing conditions.

Formulation: Lyophilized from a 0.2μm filtered solution of 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:

Antibodies:

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.