Human BACE-1 Protein 4253

$218.00 – $725.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: Thr22-Thr457

SKU: 4253parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_036236
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	The beta-site amyloid precursor protein cleaving enzyme-1 (BACE-1) initiates the generation of amyloid-β (Aβ), and the amyloid cascade leading to amyloid plaque deposition, neurodegeneration, and dementia in Alzheimer's disease (AD). Clinical failures of anti-Aβ therapies in dementia stages suggest that treatment has to start in the early, asymptomatic disease states.
molecular weight	The protein has a predicted MW of 49.5 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human BACE-1 Protein 4253

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
The beta-site amyloid precursor protein cleaving enzyme-1 (BACE-1) initiates the generation of amyloid-β (Aβ), and the amyloid cascade leading to amyloid plaque deposition, neurodegeneration, and dementia in Alzheimer's disease (AD). Clinical failures of anti-Aβ therapies in dementia stages suggest that treatment has to start in the early, asymptomatic disease states.
Protein names GTPase HRas (EC 3.6.5.2) (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed]
Gene names HRAS,HRAS HRAS1
Protein family Small GTPase superfamily, Ras family
Mass 21298Da
Function FUNCTION: Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). {ECO:0000269\|PubMed:12740440, ECO:0000269\|PubMed:14500341, ECO:0000269\|PubMed:22821884, ECO:0000269\|PubMed:9020151}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269\|PubMed:9020151};
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250\|UniProtKB:P20171}; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
Tissues TISSUE SPECIFICITY: Widely expressed. {ECO:0000269\|PubMed:14500341}.
Structure SUBUNIT: In its GTP-bound form interacts with PLCE1 (PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706). Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1 (PubMed:14500341). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (PubMed:10608844, PubMed:11598133). Interacts (active GTP-bound form) with both SHOC2 and PP1c (all isoforms) to form a tertiary complex; SHOC2 and PP1c preferably bind M-Ras/MRAS, but they also bind K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS (PubMed:35768504, PubMed:35831509, PubMed:36175670). Interacts (GTP-bound form) with MAPKAP1/SIN1; inhibiting H-Ras/HRAS activity (PubMed:35522713). {ECO:0000250\|UniProtKB:P20171, ECO:0000250\|UniProtKB:Q61411, ECO:0000269\|PubMed:10369681, ECO:0000269\|PubMed:10608844, ECO:0000269\|PubMed:11022048, ECO:0000269\|PubMed:11257115, ECO:0000269\|PubMed:11598133, ECO:0000269\|PubMed:11980706, ECO:0000269\|PubMed:14500341, ECO:0000269\|PubMed:17230191, ECO:0000269\|PubMed:18596699, ECO:0000269\|PubMed:35522713, ECO:0000269\|PubMed:35768504, ECO:0000269\|PubMed:35831509, ECO:0000269\|PubMed:36175670}.
Post-translational modification PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.; PTM: S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.; PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250}.; PTM: Fatty-acylated at Lys-170. {ECO:0000269\|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000269\|PubMed:30442762}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL (PubMed:19744486, PubMed:8626575, PubMed:8626586, PubMed:9632667). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to inhibit Ras signaling (PubMed:8626575, PubMed:8626586, PubMed:9632667). {ECO:0000269\|PubMed:19744486, ECO:0000269\|PubMed:8626575, ECO:0000269\|PubMed:8626586, ECO:0000269\|PubMed:9632667}.
Target Relevance information above includes information from UniProt accession: P01112
The UniProt Consortium

Data

Activity assay with Human BACE-1 Protein

Measured by its ability to cleave a fluorogenic peptide substrate, Mca-SEVNLDAEFRK(Dpn)RR-NH2. The specific activity is >3.5 pmol/min/µg.

The purity of Human BACE-1 is greater than 95% as determined by SEC-HPLC.

Human BACE-1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.