AGER Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, E |
---|---|
Primary Accession | Q15109 |
Reactivity | Human |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit Ig |
Calculated MW | 42803 Da |
Gene ID | 177 |
---|---|
Other Names | Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, RAGE |
Target/Specificity | This AGER antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 174-208 amino acids from the Central region of human AGER. |
Dilution | WB~~1:1000-1:2000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | AGER Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | AGER |
---|---|
Synonyms | RAGE |
Function | 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. 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 with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides. |
Cellular Location | Isoform 1: Cell membrane; Single-pass type I membrane protein Isoform 10: Cell membrane; Single-pass type I membrane protein |
Tissue Location | Endothelial cells. |

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Background
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. 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 with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.
References
Neeper M.,et al.J. Biol. Chem. 267:14998-15004(1992).
Sugaya K.,et al.Genomics 23:408-419(1994).
Abedin M.J.,et al.Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
Malherbe P.,et al.Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
Yonekura H.,et al.Biochem. J. 370:1097-1109(2003).

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