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beta-Site APP-Cleaving Enzyme 1 (BACE) antibody

Details for Product No. ABIN401041, Supplier: Log in to see
Antigen
  • BACE1
  • MGC145931
  • bace2
  • MGC68881
  • MGC68482
  • BACE2
  • C76936
  • Bace
  • ASP2
  • BACE
  • HSPC104
  • zgc:77409
  • beta-site APP-cleaving enzyme 1
  • beta-site APP-cleaving enzyme 2
  • beta-site APP cleaving enzyme 1
  • BACE1
  • MGC145931
  • LOC100232107
  • bace2
  • BACE2
  • LOC100224177
  • Bace1
  • bace1
Reactivity
Human, Mouse (Murine)
235
140
99
21
12
11
6
6
6
5
5
5
5
3
2
2
1
1
1
Host
Rabbit
196
46
6
Clonality
Polyclonal
Conjugate
Un-conjugated
8
7
4
4
4
4
3
3
3
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
160
85
76
46
26
20
19
16
16
5
2
2
2
2
1
1
Options
Supplier
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Immunogen Synthetic peptide corresponding to amino acids near the carboxyl terminus of human BACE protein
Isotype IgG
Specificity This antibody is directed against BACE protein.
Purification DEAE ion exchange chromatography
Alternative Name BACE1 (BACE Antibody Abstract)
Background Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by two proteases. APP is first cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as the substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide, which is deposited in the brains of all sufferers of Alzheimer's disease. The long-sought beta-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2) (1-4). BACE/Asp2 is a novel transmembrane aspartic protease and co-localizes with APP.Synonyms: ASP2, Aspartyl protease 2, BACE, BACE-1, Beta-secretase 1, Beta-site APP cleaving enzyme 1, Beta-site amyloid precursor protein cleaving enzyme 1, KIAA1149, Memapsin-2, Membrane-associated aspartic protease 2
Gene ID 23621
NCBI Accession NP_036236
UniProt P56817
Research Area Proteolysis / Ubiquitin, Alzheimer's Disease, Enzymes
Application Notes Western Blot: 0.5-1 μg/mL. Immunohistochemistry: 10 μg/mL.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 0.5 mg/mL (by UV absorbance at 280 nm)
Buffer 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 containing 0.02 % (w/v) Sodium Azide as preservative
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Avoid repeated freezing and thawing.
Storage -20 °C
Supplier Images
 image for anti-beta-Site APP-Cleaving Enzyme 1 (BACE) antibody (ABIN401041) anti-beta-Site APP-Cleaving Enzyme 1 (BACE) antibody
 image for anti-beta-Site APP-Cleaving Enzyme 1 (BACE) antibody (ABIN401041) anti-beta-Site APP-Cleaving Enzyme 1 (BACE) antibody (Image 2)
Background publications Hussain, Powell, Howlett, Tew, Meek, Chapman, Gloger, Murphy, Southan, Ryan, Smith, Simmons, Walsh, Dingwall, Christie: "Identification of a novel aspartic protease (Asp 2) as beta-secretase." in: Molecular and cellular neurosciences, Vol. 14, Issue 6, pp. 419-27, 2000 (PubMed).

Vassar, Bennett, Babu-Khan, Kahn, Mendiaz, Denis, Teplow, Ross, Amarante, Loeloff, Luo, Fisher, Fuller, Edenson, Lile, Jarosinski, Biere, Curran, Burgess, Louis, Collins, Treanor, Rogers, Citron: "Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE." in: Science (New York, N.Y.), Vol. 286, Issue 5440, pp. 735-41, 1999 (PubMed).

Yan, Bienkowski, Shuck, Miao, Tory, Pauley, Brashier, Stratman, Mathews, Buhl, Carter, Tomasselli, Parodi, Heinrikson, Gurney: "Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity." in: Nature, Vol. 402, Issue 6761, pp. 533-7, 1999 (PubMed).

Sinha, Anderson, Barbour, Basi, Caccavello, Davis, Doan, Dovey, Frigon, Hong, Jacobson-Croak, Jewett, Keim, Knops, Lieberburg, Power, Tan, Tatsuno, Tung, Schenk, Seubert, Suomensaari, Wang, Walker et al.: "Purification and cloning of amyloid precursor protein beta-secretase from human brain. ..." in: Nature, Vol. 402, Issue 6761, pp. 537-40, 1999 (PubMed).