Antibody data
- Antibody Data
- Antigen structure
- References [9]
- Comments [0]
- Validations [0]
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- Product number
- ABIN350071 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN350071, RRID:AB_10782160
- Product name
- anti-Amyloid beta (A4) Precursor Protein (APP) (AA 400-450) antibody
- Antibody type
- Polyclonal
- Antigen
- A synthetic peptide from aa region 400-450 of human APP conjugated to an immunogenic carrier protein was used as the antigen.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- AA 400-450
- Isotype
- IgG
- Vial size
- 500 μg
- Storage
- Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
- Handling
- Avoid freeze and thaw cycles.
Submitted references Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch.
Appican, the proteoglycan form of the amyloid precursor protein, contains chondroitin sulfate E in the repeating disaccharide region and 4-O-sulfated galactose in the linkage region.
Expression of the APP gene family in brain cells, brain development and aging.
APP gene family. Alternative splicing generates functionally related isoforms.
The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures.
Purification and tissue level of the beta-amyloid peptide precursor of rat brain.
The sequence of the two extra exons in rat preA4.
Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.
Amyloid beta protein precursor is possibly a heparan sulfate proteoglycan core protein.
Gu Y, Misonou H, Sato T, Dohmae N, Takio K, Ihara Y
The Journal of biological chemistry 2001 Sep 21;276(38):35235-8
The Journal of biological chemistry 2001 Sep 21;276(38):35235-8
Appican, the proteoglycan form of the amyloid precursor protein, contains chondroitin sulfate E in the repeating disaccharide region and 4-O-sulfated galactose in the linkage region.
Tsuchida K, Shioi J, Yamada S, Boghosian G, Wu A, Cai H, Sugahara K, Robakis NK
The Journal of biological chemistry 2001 Oct 5;276(40):37155-60
The Journal of biological chemistry 2001 Oct 5;276(40):37155-60
Expression of the APP gene family in brain cells, brain development and aging.
Sandbrink R, Mönning U, Masters CL, Beyreuther K
Gerontology 1997;43(1-2):119-31
Gerontology 1997;43(1-2):119-31
APP gene family. Alternative splicing generates functionally related isoforms.
Sandbrink R, Masters CL, Beyreuther K
Annals of the New York Academy of Sciences 1996 Jan 17;777:281-7
Annals of the New York Academy of Sciences 1996 Jan 17;777:281-7
The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures.
Shioi J, Pangalos MN, Ripellino JA, Vassilacopoulou D, Mytilineou C, Margolis RU, Robakis NK
The Journal of biological chemistry 1995 May 19;270(20):11839-44
The Journal of biological chemistry 1995 May 19;270(20):11839-44
Purification and tissue level of the beta-amyloid peptide precursor of rat brain.
Potempska A, Styles J, Mehta P, Kim KS, Miller DL
The Journal of biological chemistry 1991 May 5;266(13):8464-9
The Journal of biological chemistry 1991 May 5;266(13):8464-9
The sequence of the two extra exons in rat preA4.
Kang J, Müller-Hill B
Nucleic acids research 1989 Mar 11;17(5):2130
Nucleic acids research 1989 Mar 11;17(5):2130
Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.
Shivers BD, Hilbich C, Multhaup G, Salbaum M, Beyreuther K, Seeburg PH
The EMBO journal 1988 May;7(5):1365-70
The EMBO journal 1988 May;7(5):1365-70
Amyloid beta protein precursor is possibly a heparan sulfate proteoglycan core protein.
Schubert D, Schroeder R, LaCorbiere M, Saitoh T, Cole G
Science (New York, N.Y.) 1988 Jul 8;241(4862):223-6
Science (New York, N.Y.) 1988 Jul 8;241(4862):223-6
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