HTRA2 Human

HTRA2 Human Recombinant
Cat. No.
BT25020
Source
Escherichia Coli.
Synonyms
Serine protease HTRA2 mitochondrial, EC 3.4.21.108, High temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, Serine proteinase OMI, Serine protease 25, OMI, PARK13, PRSS25.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

HtrA2 Human Recombinant amino acids 134-458 His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 36kDa.
The HtrA2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
HtrA2, also known as Omi, is a serine protease found in mammals that exhibits protease activity at high temperatures and chaperone activity at low temperatures. Initially synthesized as a precursor protein, full-length HtrA2 is directed to the mitochondria, where it undergoes maturation through the removal of its N-terminal 133 residues. The mature HtrA2 protein comprises several key domains: a putative transmembrane domain, an inhibitor of apoptosis protein (IAP)-binding motif, and a C-terminal PDZ domain responsible for mediating protein-protein interactions. Recent studies have highlighted HtrA2's involvement in both caspase-dependent and caspase-independent cell death.
Description
Recombinant human HtrA2, encompassing amino acids 134-458 and containing a C-terminal His-tag, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain with a molecular weight of 36 kDa. Purification of HtrA2 is achieved using proprietary chromatographic techniques.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The protein is supplied at a concentration of 0.5 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 50 mM NaCl, 1 mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. Long-term storage requires freezing at -20°C. Adding a carrier protein such as 0.1% HSA or BSA is recommended for extended storage durations. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of the HtrA2 protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Serine protease HTRA2 mitochondrial, EC 3.4.21.108, High temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, Serine proteinase OMI, Serine protease 25, OMI, PARK13, PRSS25.
Source
Escherichia Coli.
Amino Acid Sequence
MAVPSPPPAS PPSQYNFIAD VVEKTAPAVV YIEILDRHPF LGREVPISNG SGFVVAADGL IVTNAHVVAD RRRVRVRLLS GDTYEAVVTA VDPVADIATL RIQTKEPLPT LPLGRSADVR QGEFVVAMGS PFALQNTITS GIVSSAQRPA RDLGLPQTNV EYIQTDAAID FGNAGGPLVN LDGEVIGVNT MKVTAGISFA IPSDRLREFL HRGEKKNSSS GISGSQRRYI GVMMLTLSPS ILAELQLREP SFPDVQHGVL IHKVILGSPA HRAGLRPGDV ILAIGEQMVQ NAEDVYEAVR TQSQLAVQIR RGRETLTLYV TPEVTEGSHH HHHH.

Product Science Overview

Structure and Function

HTRA2 is synthesized as a precursor protein and is processed to its mature form within the mitochondria. The mature protein contains a serine protease domain and a PDZ domain, which are crucial for its proteolytic activity and substrate recognition, respectively . The protein is involved in the degradation of misfolded or damaged proteins within the mitochondria, thereby maintaining mitochondrial function and integrity .

Role in Apoptosis

One of the key functions of HTRA2 is its role in apoptosis. Under stress conditions, HTRA2 is released from the mitochondria into the cytosol, where it interacts with and cleaves various substrates, including inhibitor of apoptosis proteins (IAPs). This cleavage leads to the activation of caspases, which are the executioners of apoptosis . Thus, HTRA2 acts as a pro-apoptotic factor, promoting cell death in response to cellular stress.

Clinical Significance

Mutations in the HTRA2 gene have been associated with several diseases, including Parkinson’s disease and 3-methylglutaconic aciduria, type VIII . In Parkinson’s disease, mutations in HTRA2 are thought to impair its proteolytic activity, leading to the accumulation of damaged proteins and mitochondrial dysfunction, which contribute to the degeneration of dopaminergic neurons .

Recombinant HTRA2

Recombinant HTRA2 is produced using various expression systems, such as E. coli, to study its structure, function, and role in disease. The recombinant protein is often used in biochemical assays to investigate its proteolytic activity and interactions with other proteins . For instance, recombinant HTRA2 has been shown to cleave beta-casein, a model substrate, demonstrating its protease activity .

Research Applications

HTRA2 is a subject of extensive research due to its dual role in maintaining mitochondrial homeostasis and regulating apoptosis. Studies have shown that HTRA2 is involved in the response to cellular stress and the regulation of mitochondrial dynamics . Additionally, HTRA2 is being investigated as a potential therapeutic target for diseases associated with mitochondrial dysfunction and impaired apoptosis, such as neurodegenerative diseases and cancer .

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