Anti-Human Beta Site APP Cleaving Enzyme (CT) (BACE)
| Code | Size | Price |
|---|
| LEI-B362-20ug | 20 ug | £221.00 |
Quantity:
| LEI-B362-0.1mg | 0.1 mg | £591.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Rabbit
Antibody Clonality: Polyclonal
Regulatory Status: RUO
Target Species: Human
Application: Western Blot (WB)
Shipping:
Ambient
Storage:
This polyclonal antibody is stable for at least one week when stored at 2-8°C. For long term storage aliquot in working volumes without diluting and store at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles.
Further Information
Concentration:
0.5 mg/ml
Conjugate/Tag/Label:
Purified No Carrier Protein
Format:
This polyclonal antibody is formulated in phosphate buffered saline (PBS) pH 7.4 containing 0.02% sodium azide as a preservative.
Formulation:
This polyclonal antibody is formulated in phosphate buffered saline (PBS) pH 7.4 containing 0.02% sodium azide as a preservative.
Immunogen:
PN:B365
Long Description:
Accumulation of the amyloid-b (Ab) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer?s disease. Ab peptide is generated by proteolytic cleavage of the b-amyloid protein precursor (APP) at b- and g-sites by two proteases. APP is first cleaved by b-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for g-secretase to generate the 4 kDa amyloid-b peptide, which is deposited in the brains of all suffers of Alzheimer?s disease. The long-sought b-secretase was recently identified by several groups independently and designated β-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2).1-4 BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
NCBI Gene:
23621
Target:
Beta Site APP Cleaving Enzyme
References
1. Vassar, R. et al. (1999) Science 286:735
2. Hussain, I. et al. (1999) Mol. Cell Neurosci. 14:419
3. Yan, R. et al. (1999) Nature 402:533
4. Sinha, S. et al. (1999) Nature 402:537
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