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Mouse Anti-BACE1 Recombinant Antibody (3C1C3) (CBMAB-1182-CN)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
3C1C3
Antibody Isotype
IgG1
Application
WB, ELISA, FC, IF

Basic Information

Immunogen
Purified recombinant fragment of human BACE1 (AA: 112-324) expressed in E. Coli.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IF(ICC)1:200-1:1,000
ELISA1:10,000
FC1:200-1:400

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
0.05% sodium azide
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Beta-Secretase 1
Introduction
This gene encodes a member of the peptidase A1 family of aspartic proteases. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature protease. Vassar et al. (1999) found that transient overexpression of BACE did not affect APP expression, but decreased alpha-secretase cleavage and increased beta-secretase activity in cells expressing wildtype or Swedish mutant (104760.0008) APP. BACE overexpression induced cleavage only at the known beta-secretase positions, asp1 and glu11. The BACE aspartic protease is the long-sought APP beta-secretase. This transmembrane protease catalyzes the first step in the formation of amyloid beta peptide from amyloid precursor protein. Amyloid beta peptides are the main constituent of amyloid beta plaques, which accumulate in the brains of human Alzheimer's disease patients.
Entrez Gene ID
Human23621
Mouse23821
Rat29392
UniProt ID
HumanP56817
MouseP56818
RatP56819
Alternative Names
ASP2; BACE; HSPC104
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).
Biological Process
Amyloid-beta formation Source: ARUK-UCL
Amyloid-beta metabolic process Source: UniProtKB
Amyloid fibril formation Source: Reactome
Amyloid precursor protein catabolic process Source: ARUK-UCL
Cellular response to amyloid-beta Source: Ensembl
Cellular response to copper ion Source: Ensembl
Cellular response to manganese ion Source: Ensembl
Detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
Membrane protein ectodomain proteolysis Source: UniProtKB
Positive regulation of neuron apoptotic process Source: ARUK-UCL
Prepulse inhibition Source: Ensembl
Protein processing Source: ARUK-UCL
Proteolysis Source: UniProtKB
Regulation of synaptic vesicle exocytosis Source: Ensembl
Response to lead ion Source: Ensembl
Response to radiation Source: Ensembl
Cellular Location
Endoplasmic reticulum; Trans-Golgi network; Endosome; Late endosome; Early endosome; Recycling endosome; Cell membrane; Lysosome; Cell surface; Cytoplasmic vesicle membrane; Membrane raft; Axon; Dendrite. 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:17425515, PubMed:11466313). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich 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).
Topology
Extracellular: 22-457 aa
Helical: 458-478 aa
Cytoplasmic: 479-501 aa
PTM
N-Glycosylated (PubMed:11083922, PubMed:17425515). Addition of a bisecting N-acetylglucosamine by MGAT3 blocks lysosomal targeting, further degradation and is required for maintaining stability under stress conditions (By similarity).
Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307. Acetylation by NAT8 and NAT8B is transient and deacetylation probably occurs in the Golgi. Acetylation regulates the maturation, the transport to the plasma membrane, the stability and the expression of the protein.
Palmitoylation mediates lipid raft localization.
Ubiquitinated at Lys-501, ubiquitination leads to lysosomal degradation (PubMed:27302062, PubMed:16033761, PubMed:20484053, PubMed:23109336). Monoubiquitinated and 'Lys-63'-linked polyubitinated (PubMed:20484053). Deubiquitnated by USP8; inhibits lysosomal degradation (PubMed:27302062).
Phosphorylation at Ser-498 is required for interaction with GGA1 and retrograded transport from endosomal compartments to the trans-Golgi network. Non-phosphorylated BACE1 enters a direct recycling route to the cell surface.
More Infomation

Cervellati, C., Trentini, A., Rosta, V., Passaro, A., Bosi, C., Sanz, J. M., ... & Zuliani, G. (2020). Serum beta-secretase 1 (BACE1) activity as candidate biomarker for late-onset Alzheimer’s disease. GeroScience, 42(1), 159-167.

Kumar, V., Ojha, P. K., Saha, A., & Roy, K. (2020). Exploring 2D-QSAR for prediction of beta-secretase 1 (BACE1) inhibitory activity against Alzheimer’s disease. SAR and QSAR in Environmental Research, 31(2), 87-133.

Vakilian, A., Masoumi, J., Mirzaee, S., & Khorramdelazad, H. (2019). Expression analysis of beta-secretase 1 (BACE1) enzyme in peripheral blood of patients with Alzheimer's disease. Caspian journal of internal medicine, 10(3), 276.

Pan, X., & Green, B. D. (2019). Temporal Effects of Neuron-specific beta-secretase 1 (BACE1) Knock-in on the Mouse Brain Metabolome: Implications for Alzheimer's Disease. Neuroscience, 397, 138-146.

Yaghoobi, H., Azizi, H., Banitalebi-Dehkordi, M., Rezaei, F. M., Arsang-Jnag, S., Taheri, M., & Ghafouri-Fard, S. (2019). Beta-secretase 1 (BACE1) is down-regulated in invasive ductal carcinoma of breast. Reports of biochemistry & molecular biology, 8(2), 200.

Zhang, Z., Cui, J., Gao, F., Li, Y., Zhang, G., Liu, M., ... & Li, R. (2019). Elevated cleavage of neuregulin-1 by beta-secretase 1 in plasma of schizophrenia patients. Progress in Neuro-Psychopharmacology and Biological Psychiatry, 90, 161-168.

Mazdeh, M., Komaki, A., Omrani, M. D., Gharzi, V., Sayad, A., Taheri, M., & Ghafouri-Fard, S. (2018). Expression analysis of beta-secretase 1 (BACE1) and its naturally occurring antisense (BACE1-AS) in blood of epileptic patients. Neurological Sciences, 39(9), 1565-1569.

Meakin, P. J., Mezzapesa, A., Benabou, E., Haas, M. E., Bonardo, B., Grino, M., ... & Peiretti, F. (2018). The beta secretase BACE1 regulates the expression of insulin receptor in the liver. Nature communications, 9(1), 1-14.

Shen, Y., Wang, H., Sun, Q., Yao, H., Keegan, A. P., Mullan, M., ... & Hampel, H. (2018). Increased plasma beta-secretase 1 may predict conversion to Alzheimer’s disease dementia in individuals with mild cognitive impairment. Biological psychiatry, 83(5), 447-455.

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For research use only. Not intended for any clinical use.

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