BACE2C Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9Y5Z0 |
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Other Accession | Q9NZL2 |
Clone Names | 2091509 |
Gene ID | 25825 |
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Other Names | Beta-secretase 2, Aspartic-like protease 56 kDa, Aspartyl protease 1, ASP1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Beta-site APP cleaving enzyme 2, Down region aspartic protease, DRAP, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase, BACE2, AEPLC, ALP56, ASP21 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6106a was selected from the C-term region of human BACE2C . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | BACE2 |
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Synonyms | AEPLC, ALP56, ASP21 |
Function | Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading 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. It has also been shown that it can cleave APP between residues 671 and 672 (PubMed:10591213, PubMed:11083922, PubMed:11423558, PubMed:15857888, PubMed:16816112). Involved in the proteolytic shedding of PMEL at early stages of melanosome biogenesis. Cleaves PMEL within the M-beta fragment to release the amyloidogenic PMEL luminal fragment containing M-alpha and a small portion of M-beta N-terminus. This is a prerequisite step for subsequent processing and assembly of PMEL fibrils into amyloid sheets (PubMed:23754390). Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells (PubMed:21907142). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Golgi apparatus. Endoplasmic reticulum. Endosome Melanosome. Note=Colocalizes with PMEL in stage I and II melanosomes. |
Tissue Location | Brain. Present in neurons within the hippocampus, frontal cortex and temporal cortex (at protein level). Expressed at low levels in most peripheral tissues and at higher levels in colon, kidney, pancreas, placenta, prostate, stomach and trachea. Expressed at low levels in the brain. Found in spinal cord, medulla oblongata, substantia nigra and locus coruleus. Expressed in the ductal epithelium of both normal and malignant prostate. |

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Background
Amyloid-beta peptide aggregation is a signature of Alzheimer disease and a frequent complication of adult Down syndrome patients. Amyloid-beta is generated by proteolytic processing of the amyloid precursor protein (APP) by beta- and gamma-secretase at the N and C termini, respectively. Presenilin-1 is involved in the gamma-secretase activity. BACE is a transmembrane aspartyl protease with beta-secretase activity. BACE2, also termed ALP56 has 2 pepsin-like active centers, a signal sequence, a propeptide, and a long C-terminal extension including a transmembrane domain, with expression in a wide array of tissues. Northern blot analysis revealed low expression of 2.0- and 2.6-kb BACE2 transcripts in most fetal and adult tissues, with higher expression in adult colon, kidney, pancreas, placenta, prostate, stomach, and trachea. Low levels were also detected in brain, with somewhat higher expression in medulla and spinal cord. In situ hybridization analysis of rat brain found low-level BACE2 expression in contrast to BACE expression. The BACE2 expression pattern does not appear to be consistent with that of a beta-secretase. BACE2 has been mapped to 21q22.3, within the Down syndrome critical region.

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