Sarcosine amide hydrochloride
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Sarcosine amide hydrochloride

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Category
Other Unnatural Amino Acids
Catalog number
BAT-005722
CAS number
5325-64-4
Molecular Formula
C3H8N2O·HCl
Molecular Weight
124.57
Sarcosine amide hydrochloride
Synonyms
Sar-NH2 HCl; N-Methylglycine amide hydrochloride
Appearance
Almost white powder
Purity
≥ 99% (Assay by titration on dried basis)
Melting Point
150-154 °C
Storage
Store at 2-8°C
InChI
InChI=1S/C3H8N2O.ClH/c1-5-2-3(4)6;/h5H,2H2,1H3,(H2,4,6);1H
InChI Key
VVIXOTCTYAILNP-UHFFFAOYSA-N
Canonical SMILES
CNCC(=O)N.Cl
1. Purification and antigenicity of two recombinant forms of Boophilus microplus yolk pro-cathepsin expressed in inclusion bodies
Alexandre T Leal, et al. Protein Expr Purif. 2006 Jan;45(1):107-14. doi: 10.1016/j.pep.2005.07.009. Epub 2005 Aug 8.
The tick Boophilus microplus is a bovine ectoparasite present in tropical and subtropical areas of the world and the use of vaccines is a promising method for tick control. BYC is an aspartic proteinase found in eggs that is involved in the embryogenesis of B. microplus and was proposed as an important antigen in the development of an anti-tick vaccine. The cDNA of BYC was amplified by PCR and cloned for expression in two forms with and without thioredoxin fusion protein (Trx), coding recombinant proteins named rBYC-Trx and rBYC, respectively. Expression, solubility, and yields of the two forms were analyzed. The recombinant proteins were expressed in inclusion bodies (IBs) and three denaturant agents (N-lauroyl sarcosine, guanidine hydrochloride, and urea) were tested for IBs solubilization. The N-lauroyl sarcosine solubilized 90.4 and 92.4% of rBYC-Trx and rBYC IBs, respectively, and was the most efficient denaturant. Two recombinant forms were affinity-purified by Ni2+-Sepharose under denaturing conditions. After dialysis, the yield of soluble protein was 84.1% for r-BYC-Trx and 5.9% for rBYC. These proteins were immune-reactive against sera from rabbit, mouse, and bovine previously immunized with native BYC, which confirms the antigenicity of the recombinant BYCs expressed in the Escherichia coli system.
2. Putting the Piezolyte Hypothesis under Pressure
Christina M Papini, Pranav P Pandharipande, Catherine A Royer, George I Makhatadze Biophys J. 2017 Sep 5;113(5):974-977. doi: 10.1016/j.bpj.2017.07.012. Epub 2017 Aug 10.
A group of small molecules that stabilize proteins against high hydrostatic pressure has been classified as piezolytes, a subset of stabilizing cosolutes. This distinction would imply that piezolytes counteract the effects of high hydrostatic pressure through effects on the volumetric properties of the protein. The purpose of this study was to determine if cosolutes proposed to be piezolytes have an effect on the volumetric properties of proteins through direct experimental measurements of volume changes upon unfolding of model proteins lysozyme and ribonuclease A, in solutions containing varying cosolute concentrations. Solutions containing the proposed piezolytes glutamate, sarcosine, and betaine were used, as well as solutions containing the denaturants guanidinium hydrochloride and urea. Changes in thermostability were monitored using differential scanning calorimetry whereas changes in volume were monitored using pressure perturbation calorimetry. Our findings indicate that increasing stabilizing cosolute concentration increases the stability and transition temperature of the protein, but does not change the temperature dependence of volume changes upon unfolding. The results suggest that the pressure stability of a protein in solution is not directly affected by the presence of these proposed piezolytes, and so they cannot be granted this distinction.
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