Recombinant Human beta-site APP-cleaving enzyme 1 Protein, His tagged
Cat.No. : | BACE1-13H |
Product Overview : | Recombinant human BACE-1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
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Description : | 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. 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. |
Source : | Baculovirus |
Species : | Human |
Tag : | C-His |
Protein length : | 22-457aa |
Form : | Liquid |
Bio-activity : | > 5 pmol/min/μg in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25 centigrade. |
Molecular Mass : | 49.2 kDa |
AA Sequence : | TQHGIRLPLRSGLGGAPLGLRLPRE TDEEPEEPGRRGSFVEMVDNLRGKS GQGYYVEMTVGSPPQTLNILVDTGS SNFAVGAAPHPFLHRYYQRQLSSTY RDLRKGVYVPYTQGKWEGELGTDLV SIPHGPNVTVRANIAAITESDKFFI NGSNWEGILGLAYAEIARPDDSLEP FFDSLVKQTHVPNLFSLQLCGAGFP LNQSEVLASVGGSMIIGGIDHSLYT GSLWYTPIRREWYYEVIIVRVEING QDLKMDCKEYNYDKSIVDSGTTNLR LPKKVFEAAVKSIKAASSTEKFPDG FWLGEQLVCWQAGTTPWNIFPVISL YLMGEVTNQSFRITILPQQYLRPVE DVATSQDDCYKFAISQSSTGTVMGA VIMEGFYVVFDRARKRIGFAVSACH VHDEFRTAAVEGPFVTLDMEDCGYN IPQTDESTLMT |
Endotoxin : | < 1 EU/μg, determined by LAL method. |
Purity : | > 90% by SDS-PAGE |
Applications : | SDS-PAGE, Enzyme Activity |
Storage : | Can be stored at +2 to +8 centigrade for 1 week. For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles. |
Concentration : | 0.5 mg/mL (determined by BCA assay) |
Storage Buffer : | Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol |
Notes : | For research use only. This product is not intended or approved for human, diagnostics or veterinary use. |
References : | 1. Andrew RJ., et al. (2013) Proc Natl Acad Sci U S A. 114:E9665-E9674. 2. Brendel M., et al. (2018) Theranostics. 8:4957-4968. |
Gene Name : | BACE1 beta-site APP-cleaving enzyme 1 [ Homo sapiens (human) ] |
Official Symbol : | BACE1 |
Synonyms : | BACE1; beta-site APP-cleaving enzyme 1; BACE, beta site APP cleaving enzyme; beta-secretase 1; asp 2; memapsin-2; APP beta-secretase; aspartyl protease 2; beta-site APP cleaving enzyme 1; beta-secretase 1 precursor variant 1; transmembrane aspartic proteinase Asp2; membrane-associated aspartic protease 2; beta-site amyloid beta A4 precursor protein-cleaving enzyme; ASP2; BACE; HSPC104; FLJ90568; KIAA1149; |
Gene ID : | 23621 |
mRNA Refseq : | NM_012104 |
Protein Refseq : | NP_036236 |
MIM : | 604252 |
UniProt ID : | P56817 |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewSuch support ensures researchers have access to reliable tools and expertise, facilitating their investigations into the functions, mechanisms, and disease relevance of BACE1 protein.
A manufacturer can serve as a collaborative partner, engaging in discussions, and exchanging knowledge with researchers.
Using BACE1 protein in trials provides advantages such as its involvement in cellular processes and its disease associations.
Q&As (5)
Ask a questionYes, several clinical trials are underway to assess the safety and efficacy of BACE1 inhibitors in treating Alzheimer's disease.
BACE1 is implicated in Alzheimer's disease as it initiates the cleavage of APP, leading to the formation of beta-amyloid plaques, a hallmark of the disease.
BACE1 inhibitors may slow down or prevent the accumulation of beta-amyloid plaques, potentially delaying the progression of Alzheimer's disease.
Yes, several clinical trials are underway to assess the safety and efficacy of BACE1 inhibitors in treating Alzheimer's disease.
Yes, BACE1 inhibitors are being explored as potential therapeutic agents for Alzheimer's disease to reduce the production of beta-amyloid peptides.
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