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AGER recombinant protein :: Advanced glycosylation end product-specific receptor Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS1265116
SDS-PAGE
Unit / Price
0.01 mg  /  $110 +1 FREE 8GB USB
0.05 mg  /  $190 +1 FREE 8GB USB
0.1 mg  /  $285 +1 FREE 8GB USB
0.2 mg  /  $460 +1 FREE 8GB USB
0.5 mg  /  $750 +1 FREE 8GB USB
1 mg  /  $1,180 +1 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Advanced glycosylation end product-specific receptor (AGER), Recombinant Protein

 Also Known As   

Recombinant Human Advanced glycosylation end product-specific receptor

 Product Synonym Names    Receptor for advanced glycosylation end products
 Product Gene Name   

AGER recombinant protein

[Similar Products]
 Product Synonym Gene Name    RAGE [Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 Sequence Positions    23-342aa; Extracellular Domain
 Sequence    AQNITARIGE PLVLKCKGAP KKPPQRLEWK LNTGRTEAWK VLSPQGGGPW DSVARVLPNG SLFLPAVGIQ DEGIFRCQAM NRNGKETKSN YRVRVYQIPG KPEIVDSASE LTAGVPNKVG TCVSEGSYPA GTLSWHLDGK PLVPNEKGVS VKEQTRRHPE TGLFTLQSEL MVTPARGGDP RPTFSCSFSP GLPRHRALRT APIQPRVWEP VPLEEVQLVV EPEGGAVAPG GTVTLTCEVP AQPSPQIHWM KDGVPLPLPP SPVLILPEIG PQDQGTYSCV ATHSSHGPQE SRAVSISIIE PGEEGPTAGS VGGSGLGTLA
 OMIM    600214
 3D Structure    ModBase 3D Structure for Q15109
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 Host    E Coli
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of AGER recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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Related Product Information for AGER recombinant protein

   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. 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. 4 Publications
 Product Categories/Family for AGER recombinant protein    Immunology
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 SDS-PAGE of AGER recombinant protein    AGER recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for AGER. It may not necessarily be applicable to this product.
 NCBI GI #    10835203
 NCBI GeneID    177
 NCBI Accession #    NP_001127.1 [Other Products]
 NCBI GenBank Nucleotide #    NM_001136.4 [Other Products]
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 UniProt Primary Accession #    Q15109 [Other Products]
 UniProt Secondary Accession #    Q15279; Q3L1R4; Q3L1R5; Q3L1R6; Q3L1R7; Q3L1R8; Q3L1S0; A2BFI7; A6NKF0; A7Y2U9; B0V176 [Other Products]
 UniProt Related Accession #    Q15109 [Other Products]
 Molecular Weight    38.1kD
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 NCBI Official Full Name    advanced glycosylation end product-specific receptor isoform 1
 NCBI Official Synonym Full Names    advanced glycosylation end-product specific receptor
 NCBI Official Symbol    AGER [Similar Products]
 NCBI Official Synonym Symbols   
RAGE; SCARJ1
[Similar Products]
 NCBI Protein Information    advanced glycosylation end product-specific receptor
 UniProt Protein Name    Advanced glycosylation end product-specific receptor
 UniProt Synonym Protein Names   
Receptor for advanced glycosylation end products
 Protein Family    Advanced glycosylation end product-specific receptor
 UniProt Gene Name    AGER [Similar Products]
 UniProt Synonym Gene Names    RAGE [Similar Products]
 UniProt Entry Name    RAGE_HUMAN
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 NCBI Summary for AGER    The advanced glycosylation end product (AGE) receptor encoded by this gene is a member of the immunoglobulin superfamily of cell surface receptors. It is a multiligand receptor, and besides AGE, interacts with other molecules implicated in homeostasis, development, and inflammation, and certain diseases, such as diabetes and Alzheimer's disease. Many alternatively spliced transcript variants encoding different isoforms, as well as non-protein-coding variants, have been described for this gene (PMID:18089847). [provided by RefSeq, May 2011]
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 UniProt Comments for AGER    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 (). 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.
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Product References and Citations for AGER recombinant protein

   Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins.Neeper M., Schmidt A.M., Brett J., Yan S.D., Wang F., Pan Y.C., Elliston K., Stern D., Shaw A.J. Biol. Chem. 267:14998-15004(1992) Three genes in the human MHC class III region near the junction with the class II gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3.Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A., Inoko H., Ikemura T.Genomics 23:408-419(1994) Molecular heterogeneity of the receptor for advanced glycation endproducts.Abedin M.J., Yonekura H., Migita H., Karasawa J., Yamamoto Y., Yamamoto H.cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products (RAGE) and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein.Malherbe P., Richards J., Gaillard H., Thompson A., Diener C., Schuler A., Huber G.Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury.Yonekura H., Yamamoto Y., Sakurai S., Petrova R.G., Abedin J., Li H., Yasui K., Takeuchi M., Makita Z., Takasawa S., Okamoto H., Watanabe T., Yamamoto H.Biochem. J. 370:1097-1109(2003) Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.Genome Res. 13:2621-2636(2003) Identification, classification, and expression of RAGE gene splice variants.Hudson B.I., Carter A.M., Harja E., Kalea A.Z., Arriero M., Yang H., Grant P.J., Schmidt A.M.FASEB J. 22:1572-1580(2008) Alternative splicing of the RAGE cytoplasmic domain regulates cell signaling and function.Jules J., Maiguel D., Hudson B.I.PLoS ONE 8:E78267-E78267(2013) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003)
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 Research Articles on AGER    1. The present study revealed that the RAGE G82S polymorphism was associated with chronic periodontitis in the non-diabetes mellitus group but not in the diabetes mellitus group.
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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Products associated with AGER recombinant proteinPathways associated with AGER recombinant protein
 Reference Product  PubMed Publications
 HMGB1 recombinant protein  >10 publications with AGER and HMGB1
 S100B recombinant protein  >3 publications with AGER and S100B
 NFKB1 recombinant protein  >1 publications with AGER and NFKB1
 ITGB2 recombinant protein  >1 publications with AGER and ITGB2
 Products by Pathway  Pathway Diagram
 AGE-RAGE Signaling Pathway In Diabetic Complications antibodies  AGE-RAGE Signaling Pathway In Diabetic Complications Diagram
 AGE-RAGE Signaling Pathway In Diabetic Complications antibodies  AGE-RAGE Signaling Pathway In Diabetic Complications Diagram
 AGE/RAGE Pathway antibodies  AGE/RAGE Pathway Diagram
 Activated TLR4 Signalling Pathway antibodies  Activated TLR4 Signalling Pathway Diagram
 Advanced Glycosylation Endproduct Receptor Signaling Pathway antibodies  Advanced Glycosylation Endproduct Receptor Signaling Pathway Diagram
 Cytosolic Sensors Of Pathogen-associated DNA Pathway antibodies  Cytosolic Sensors Of Pathogen-associated DNA Pathway Diagram
 DEx/H-box Helicases Activate Type I IFN And Inflammatory Cytokines Production Pathway antibodies  DEx/H-box Helicases Activate Type I IFN And Inflammatory Cytokines Production Pathway Diagram
 Immune System Pathway antibodies  Immune System Pathway Diagram
 Innate Immune System Pathway antibodies  Innate Immune System Pathway Diagram
 MyD88 Cascade Initiated On Plasma Membrane Pathway antibodies  MyD88 Cascade Initiated On Plasma Membrane Pathway Diagram
Diseases associated with AGER recombinant proteinOrgans/Tissues associated with AGER recombinant protein
 Disease Name  Pubmed Publications
 Lung Diseases Antibodies  >47 publications with AGER and Lung Diseases
 Inflammation Antibodies  >42 publications with AGER and Inflammation
 Cardiovascular Diseases Antibodies  >40 publications with AGER and Cardiovascular Diseases
 Carcinoma Antibodies  >30 publications with AGER and Carcinoma
 Prenatal Exposure Delayed Effects Antibodies  >22 publications with AGER and Prenatal Exposure Delayed Effects
 Heart Diseases Antibodies  >19 publications with AGER and Heart Diseases
 Atherosclerosis Antibodies  >16 publications with AGER and Atherosclerosis
 Necrosis Antibodies  >14 publications with AGER and Necrosis
 Fibrosis Antibodies  >14 publications with AGER and Fibrosis
 Lung Neoplasms Antibodies  >13 publications with AGER and Lung Neoplasms
 Organ/Tissue Name  Pubmed Publications
 Lung Antibodies  >44 publications with AGER and Lung
 Lymph Node Antibodies  >33 publications with AGER and Lymph Node
 Heart Antibodies  >22 publications with AGER and Heart
 Connective Tissue Antibodies  >13 publications with AGER and Connective Tissue
 Embryonic Tissue Antibodies  >11 publications with AGER and Embryonic Tissue
 Eye Antibodies  >8 publications with AGER and Eye
 Thymus Antibodies  >7 publications with AGER and Thymus
 Intestine Antibodies  >6 publications with AGER and Intestine
 Ovary Antibodies  >6 publications with AGER and Ovary
 Stomach Antibodies  >4 publications with AGER and Stomach
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