Recombinant Streptococcus equi subsp. zooepidemicus IgG endopeptidase (ideZ)

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Code CSB-EP3597GOM
Abbreviation Recombinant Streptococcus equi subsp. zooepidemicus ideZ protein
MSDS
Size $388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
ideZ
Uniprot No.
Research Area
others
Species
Streptococcus equi subsp. zooepidemicus
Source
E.coli
Expression Region
35-349aa
Target Protein Sequence
DDYQRNAAEVYAKEVPHQITSVWTKGVTPLTPEQFRYNNEDVIHAPYLAHQGWYDITKVFDGKDNLLCGAATAGNMLHWWFDQNKTEIEAYLSKHPEKQKIIFNNQELFDLKAAIDTKDSQTNSQLFNYFRDKAFPNLSARQLGVMPDLVLDMFINGYYLNVFKTQSTDVNRPYQDKDKRGGIFDAVFTRGDQTTLLTARHDLKNKGLNDISTIIKQELTEGRALALSHTYANVSISHVINLWGADFNAEGNLEAIYVTDSDANASIGMKKYFVGINAHGHVAISAKKIEGENIGAQVLGLFTLSSGKDIWQKLS
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
37.3 kDa
Protein Length
Full Length of Mature Protein
Tag Info
C-terminal 13xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

IdeZ is a protease that has been identified as a homolog of IdeS, which is an immunoglobulin-degrading enzyme found in Streptococcus pyogenes [1]. IdeZ shares 99% amino acid sequence identity with IdeE and is more closely related to the Mac-2 protein of S. pyogenes [1]. It has been reported that IdeZ has the same specificity as IdeS but exhibits improved activity towards certain subclasses of immunoglobulin G (IgG) and has been utilized for the characterization of Fc fusion proteins [2]. Furthermore, IdeZ has been implicated in gene therapy, particularly in the context of adeno-associated virus (AAV) gene therapy, where it has shown potential similar to IdeS [3]. Additionally, IdeZ has been used in research to release the Fab portion of antibodies by treating them with IdeZ protease [4]. Moreover, IdeZ has been employed in the production of subunit liquid chromatography-mass spectrometry analysis by coupling with enzymes to produce specific subunits [5].

References:
[1] U. Pawel-Rammingen, "Streptococcal ides and its impact on immune response and inflammation", Journal of Innate Immunity, vol. 4, no. 2, p. 132-140, 2012. https://doi.org/10.1159/000332940
[2] R. O’Flaherty, I. Trbojević‐Akmačić, G. Greville, P. Rudd, & G. Lauc, "The sweet spot for biologics: recent advances in characterization of biotherapeutic glycoproteins", Expert Review of Proteomics, vol. 15, no. 1, p. 13-29, 2017. https://doi.org/10.1080/14789450.2018.1404907
[3] D. Gross, N. Tedesco, C. Leborgne, & G. Ronzitti, "Overcoming the challenges imposed by humoral immunity to aav vectors to achieve safe and efficient gene transfer in seropositive patients", Frontiers in Immunology, vol. 13, 2022. https://doi.org/10.3389/fimmu.2022.857276
[4] J. Earnest, K. Basore, V. Roy, A. Bailey, D. Wang, G. Alteret al., "Neutralizing antibodies against mayaro virus require fc effector functions for protective activity", The Journal of Experimental Medicine, vol. 216, no. 10, p. 2282-2301, 2019. https://doi.org/10.1084/jem.20190736
[5] T. Morgan, C. Jakes, H. Brouwer, S. Millán-Martín, J. Chervet, K. Cooket al., "Inline electrochemical reduction of nistmab for middle-up subunit liquid chromatography-mass spectrometry analysis", The Analyst, vol. 146, no. 21, p. 6547-6555, 2021. https://doi.org/10.1039/d1an01184g

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