Streptolysin-O

Streptolysin-O Streptococcus Pyogenes Recombinant
Cat. No.
BT21849
Source
Escherichia Coli.
Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
Appearance
Sterile Filtered white lyophilized powder.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.
The Streptolysin-O is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Streptolysin-O is a toxin activated by sulfhydryl groups. It creates pores in cell membranes that contain cholesterol, causing the cells to break down. When it attaches to a membrane, the Streptolysin-O molecule changes shape, allowing it to insert itself into the membrane and form a pore complex. Cholesterol appears to be essential for the toxin to bind to membranes, insert itself, and create pores. Oxidation can deactivate Streptolysin-O, and this process is reversible.
Description
Recombinant Streptococcus Pyogenes Streptolysin-O, produced in E.coli, is a single chain polypeptide. It is not glycosylated and consists of 538 amino acids, resulting in a molecular weight of 60.1kDa. The purification of Streptolysin-O is achieved through a proprietary chromatography method.
Physical Appearance
White, lyophilized powder that has been sterilized through filtration.
Formulation
The Streptolysin-O protein solution was filtered to 0.2µm and concentrated. It was then lyophilized in a buffer of PBS at a pH of 7.4.
Solubility
To reconstitute the lyophilized Streptolysin-O, it is recommended to dissolve it in sterile 18M-cm H₂O to a concentration of at least 100µg/ml. This solution can then be further diluted with other aqueous solutions as needed.
Stability
Lyophilized Streptolysin-O remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, Streptolysin-O should be stored at 4°C for a period of 2 to 7 days. For extended storage, it is advisable to add a carrier protein such as HSA or BSA at a concentration of 0.1%. Avoid repeated cycles of freezing and thawing.
Purity
The purity of the protein is greater than 97.0% as determined by Reverse Phase High Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
Source
Escherichia Coli.
Amino Acid Sequence
NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.

Product Science Overview

Structure and Function

Streptolysin O is a member of the thiol-activated cytolysin family, which means its activity is dependent on the presence of thiol groups. The toxin is known for its ability to form pores in cholesterol-containing lipid membranes, leading to cell lysis. This pore-forming activity is crucial for the bacterium’s ability to invade host tissues and evade the immune system .

Recombinant Expression

Recombinant Streptolysin O is produced by expressing the SLO gene in Escherichia coli. This method allows for the production of large quantities of the toxin, which can be used for research and diagnostic purposes. The recombinant protein retains the full native sequence of SLO, ensuring that it mimics the natural toxin’s properties .

Applications

Recombinant Streptolysin O has several applications in scientific research:

  1. Cell Permeabilization: SLO is used to permeabilize cell membranes, allowing researchers to introduce molecules such as antisense oligonucleotides into cells .
  2. Cholesterol Studies: The toxin’s ability to form pores in cholesterol-containing membranes makes it a valuable tool for studying cholesterol’s role in cell membranes .
  3. Protein Labeling: SLO can be used to label proteins inside living cells with external fluorophores, aiding in various imaging techniques .
Immunogenicity

One of the distinguishing features of Streptolysin O is its immunogenicity. Unlike Streptolysin S, which is non-immunogenic, SLO can elicit an immune response in the host. This property is leveraged in diagnostic assays to detect antibodies against Streptococcus pyogenes, helping in the diagnosis of infections caused by this bacterium .

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