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BACE Antibody
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- 实验流程
- 背景知识
Application 
| WB, ICC, E |
|---|---|
| Primary Accession | P56817 |
| Other Accession | AF190725, 6118538 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 55764 Da |
| Concentration (mg/ml) | 1 mg/mL |
| Conjugate | Unconjugated |
| Application Notes | BACE can be used for detection of BACE by Western blot at 1 µg/mL. Antibody can also be used for immunocytochemistry starting at 10 µg/mL. |
| Gene ID | 23621 |
|---|---|
| Other Names | BACE Antibody: ASP2, BACE, HSPC104, KIAA1149, Beta-secretase 1, Aspartyl protease 2, ASP2, beta-site APP-cleaving enzyme 1 |
| Target/Specificity | BACE1; |
| Reconstitution & Storage | BACE antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | BACE Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | BACE1 (HGNC:933) |
|---|---|
| Synonyms | BACE, KIAA1149 |
| Function | Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (PubMed:10656250, PubMed:10677483, PubMed:20354142). Cleaves CHL1 (By similarity). |
| Cellular Location | Cell membrane; Single-pass type I membrane protein Golgi apparatus, trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane raft {ECO:0000250|UniProtKB:P56818}. Lysosome. Late endosome. Early endosome. Recycling endosome. Cell projection, axon {ECO:0000250|UniProtKB:P56818}. Cell projection, dendrite {ECO:0000250|UniProtKB:P56818}. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (PubMed:11466313, PubMed:17425515). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine which blocks targeting to late endosomes and lysosomes (By similarity) Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (PubMed:15886016). {ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17425515} |
| Tissue Location | Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
BACE Antibody: 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 substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide, which is deposited in the brains of all suffers 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). BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.
REFERENCES
Vassar R, Bennett BD, Babu-Khan S, et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999;286:735-41
Hussain I, Powell D, Howlett DR , et al. Identification of a novel aspartic protease (Asp 2) as β-secretase. Mol Cell Neurosci 1999;14:419-27
Yan R, Bienkowski MJ, Shuck ME, et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature 1999;402:533-7
Sinha S, Anderson JP, Barbour R, et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 1999;402:537-40 (WD0500)
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