Analytical Data
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Gene name
CTH
- Application
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Alternative Names
CTH;Cystathionine gamma-lyase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P32929
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Expression Region
1-405aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS
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Molecular Weight
47 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CTH recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and molecular biology. CTH, or cystathionine gamma-lyase, is an enzyme involved in the transsulfuration pathway, which plays a crucial role in the metabolism of sulfur-containing amino acids. This pathway is essential for the synthesis of important biomolecules, such as cysteine and hydrogen sulfide, both of which are vital for cellular function and signaling. Disruptions in CTH activity have been linked to various diseases, including cardiovascular disorders, neurodegenerative diseases, and cancer, making it a promising target for therapeutic interventions. The ability to produce CTH as a recombinant protein allows for detailed studies of its structure, function, and regulation, facilitating the development of novel diagnostic and therapeutic strategies. Additionally, understanding the biochemical properties of CTH can aid in the exploration of its role in cellular homeostasis and disease progression. Research into CTH recombinant proteins not only enhances our fundamental understanding of enzymatic processes but also opens new avenues for innovative treatments that harness the biological activities of this important enzyme. As such, ongoing studies focus on optimizing the production and characterization of CTH recombinant proteins, aiming to unlock their full potential in both scientific research and clinical applications.
