Human Recombinant BACE1 protein (V2LY-0526-LY2283)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Protein Construction
This product is Human Recombinant BACE1 protein consist of Amino Acid: 1-457 and predicts a molecular mass of 49 kDa.
Molecule Mass
49 kDa
Verified
HPLC
Sequence
Amino Acid: 1-457
Species
Human

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

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Beta-Secretase 1
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.

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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