TY - JOUR. T1 - Purification and characterization of chymotrypsin-like enzyme from rat plasma. AU - Kumar, R. Senthil. AU - Pattabiraman, T. N.. PY - 1996/7/1. Y1 - 1996/7/1. N2 - A chymotrypsin-like enzyme was purified from rat plasma, involving ammonium sulfate fractionation and chromatographgy on CM-sephadex and red sepharose. The purified enzyme effectively hydrolysed the ester substrates for chymotrypsin (N-acetyl L-tyrosine ethyl ester and N-acetyl L-tryptophan ethyl ester). The Km values for the two substrates were 2.2×10-3M and 9.0×10-3M respectively. The hydrolytic activity of the enzyme was inhibited by phenylmethyl sulfonyl fluoride and tosylphenylalanine chloromethylketone, suggesting the presence of serine and histidine at the active centre. The enzyme exhibited anionic nature and possessed a high molecular weight (MW 71,000) as observed by gel exclusion chromatography on Sephadex G-200. The enzyme was stable upon exposure to pH 7.0-9.0, but was inactivated upon heat treatment at ...
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TY - JOUR. T1 - Selection by phage display of a mustard chymotrypsin inhibitor toxic to pea aphid.. AU - Ceci, L.R.. AU - Volpicella, M.. AU - Conti, S.. AU - Gallerani, R.. AU - Beekwilder, M.J.. AU - Jongsma, M.A.. PY - 2003. Y1 - 2003. N2 - The mustard trypsin inhibitor, MTI-2, is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for lepidopteran insects, but has low activity against aphids. In an attempt to improve the activity of the inhibitor towards aphids, a library of inhibitor variants was constructed and cloned into the pRlac3 phagemid vector. The library of 9.3 107 independent colonies was created by randomisation of a stretch of five consecutive codons in the reactive site. Repeated selection rounds against bovine trypsin and chymotrypsin allowed the identification of novel, MTI-2 derived, antitrypsin and antichymotrypsin inhibitors. Chy8, the selected variant with highest affinity for bovine chymotrypsin (Ki = 32 nm versus ,1000 nm for the ...
1MTN: Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
1OXG: Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution.
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Trypsin and chymotrypsin activity of the intestinal content in germfree, monoassociated and conventional rabbits.: Trypsin (T) and chymotrypsin (CHT) activities
Chymotrypsin is a highly-purified serine endopeptidase derived from bovine pancreas that preferentially hydrolyzes at the carboxyl side of aromatic amino acids: Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. Chymotrypsin activity is optimal in the pH range of 7.0-9.0. This sequencing grade enzyme can be used alone or in combination with other proteases to produce protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or MS/MS spectral matching. It is suitable for digestion reactions in-solution or in-gel.. ...
80700-19-2 - Chymotrypsin inhibitor (potato 1 reduced) - Searchable synonyms, formulas, resource links, and other chemical information.
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Based on summation of Coulombic interactions, a model is developed for finite-length dipole potentials of mean force in a salt-free dielectric continuum. Point-dipole and finite-length dipole potentials of mean force are compared for protein-protein interactions using parameters for bovine alpha-chymotrypsin. The two approximations made in the commonly used analytical point-dipole potentials of mean force are not valid at distances near contact.
TRYPSIN -CHYMOTRYPSIN Trypsin + Chymotrypsin, a combination of therapeutic enzymes, are prescribed for the treatment of active inflammatory edema associated with post-surgical wounds, traumatic injuries, pelvic inflammatory disorders and sciatica.
Definition : Clinical chemistry reagents intended to perform qualitative and/or quantitative chemical analyses of body fluids (typically serum) to determine the level of the enzyme chymotrypsin, particularly chymotrypsin II, the more common of the two forms of chymotrypsin in blood. Chymotrypsin levels in serum are mostly determined to assess pancreatic diseases (e.g., acute pancreatitis) and renal failures in adults; elevated levels may be present in cord blood of infants with cystic fibrosis.. Entry Terms : Chymotrypsin Determination Reagents , Reagents, Clinical Chemistry, Enzyme, Chymotrypsin. UMDC code : 18880 ...
Definition : Clinical chemistry reagents intended to perform qualitative and/or quantitative chemical analyses of body fluids (typically serum) to determine the level of the enzyme chymotrypsin, particularly chymotrypsin II, the more common of the two forms of chymotrypsin in blood. Chymotrypsin levels in serum are mostly determined to assess pancreatic diseases (e.g., acute pancreatitis) and renal failures in adults; elevated levels may be present in cord blood of infants with cystic fibrosis.. Entry Terms : Chymotrypsin Determination Reagents , Reagents, Clinical Chemistry, Enzyme, Chymotrypsin. UMDC code : 18880 ...
Chymotrypsin containing medications, Chymotrypsin indications and usages ATC and ICD codes, combinations with other active ingredients and trade names information from Drugs-about.com
Sigma-Aldrich offers abstracts and full-text articles by [Richárd Szmola, Melinda Bence, Andrea Carpentieri, András Szabó, Catherine E Costello, John Samuelson, Miklós Sahin-Tóth].
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We report a functional protease assay in which liquid crystals (LCs) are used as signal reporters to transduce the test results into optical signals. In this assay, an oligopeptide substrate (CLSELDDRADALQAGASQFESSAAKLKRKYWWKNLK) is used as a probe. This oligopeptide can be cleaved by α-chymotrypsin at multiple locations and become smaller fragments after the cleavage. When the original oligopeptide is immobilized on a solid surface, its long flexible oligopeptide chain is able to influence the orientation of a thin layer of LC supported on the surface, as is evident as a bright spot on the surface. In contrast, when the shorter oligopeptide fragments are immobilized on the same surface, their shorter, less flexible chains cannot disrupt the orientation of LC, and a dark spot is observed. On the basis of the dark or bright signal from LC, α-chymotrypsin in buffer solution or complex media such as chicken broth can be detected by using the naked eye. However, when the incubation time is 3. h, ...
BioAssay record AID 750162 submitted by ChEMBL: Inhibition of human 20S proteasome chymotrypsin like activity using Suc-Leu-Leu-Val-Tyr-AMC as substrate measured over 10 mins by fluorescence assay.
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BioAssay record AID 52301 submitted by ChEMBL: Compound was evaluated for the first order rate constant for the reactivation of Chymotrypsin in pH 7.6, 0.2 M phosphate buffer at 34.4 degrees C in D2O.
The primary specificity residue of a substrate or an inhibitor, called the P1 residue, is responsible for the proper recognition by the cognate enzyme. This residue enters the S1 pocket of the enzyme and establishes contacts (up to 50%) inside the proteinase substrate cavity, strongly affecting its specificity. To analyze the influence on bovine α-chymotrypsin substrate activity, aromatic non-proteinogenic amino acid residues in position P1 with the sequence Ac-Phe-Ala-Thr-XAnb 5,2-NH2 were introduced: L-pyridyl alanine (Pal), 4-nitrophenylalanine - Phe(p-NO2), 4-aminophenylalanine - Phe(p- NH2), 4-carboxyphenylalanine Phe(p-COOH), 4-guanidine phenylalanine - Phe(p-guanidine), 4-methyloxycarbonylphenylalanine - Phe(p-COOMe), 4-cyanophenylalanine - Phe(p-CN), Phe, Tyr. The effect of the additional substituent at the phenyl ring of the Phe residue was investigated. All peptides contained an amide of 5-amino-2-nitrobenzoic acid, which served as a chromophore. Kinetic parameters (kcat, KM and ...
Sep 30, 2019· Chymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases. It uses an active serine residue to perform hydrolysis on the C-terminus of the aromatic amino acids of other proteins. Chymotrypsin is a protease enzyme that cleaves on the C-terminal phenylalanine (F), tryptophan (W), and tyrosine (Y) on peptide ...
Staphylococcus aureus; pan ID: SAUPAN004564000; symbol: splC; products: serine protease SplC, serine protease, peptidase S1 and S6, chymotrypsin/Hap, peptidase S1 and S6 chymotrypsin/Hap, S1B family serine protease SplC, serine proteinase; orthologs: COL: SACOL1867 (splC), N315: SA1629 (splC), NCTC8325: SAOUHSC_01939, Newman: NWMN_1704 (splC)
Protein features are: Peptidase S1/S6, chymotrypsin/Hap; Peptidase S1/S6, chymotrypsin/Hap, active site; Peptidase S1A, chymotrypsin-type; Peptidase cysteine/serine, trypsin-like ...
This test looks for two enzymes from the pancreas, to find out how well the pancreas is working. This test is used for people with cystic fibrosis.
Biochemical characterizationof thc pathway enzymes.(A) ThcE4/ThcD: FTMS spectra of chymotryptic digests ASSCDCSLY andGGCESCSYEGDEAE of ThcE4 modified by ThcD. E
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Scientist John Northrop crystallized chymotrypsin in the early 1930s.. In the following years, other scientists contributed to the characterization ...
Looking for online definition of Chymotrypsin B in the Medical Dictionary? Chymotrypsin B explanation free. What is Chymotrypsin B? Meaning of Chymotrypsin B medical term. What does Chymotrypsin B mean?
Most recent works on chymotrypsins have been focused on marine animals and insects. However, no study was reported in chelicerate. Scorpion chymotrypsin-like protease (SCP) was purified to homogeneity from delipidated hepatopancreases. The protease NH2-terminal sequence exhibited more than 60% monoacids identity with those of insect putative peptidases. The protease displayed no sequence homology with classical proteases. From this point of view, the protease recalls the case of the scorpion lipase which displayed no sequence homology with known lipases. The scorpion amylase purified and characterized by our time, has an amino-acids sequence similar to those of mammalian amylases. The enzyme was characterized with respect its biochemical properties: it was active on a chymotrypsin substrate and had an apparent molecular mass of 25 kDa, like the classically known chymotrypsins. The dependence of the SCP activity and stability on pH and temperature was similar to that of mammalian chymotrypsin proteases.
Most recent works on chymotrypsins have been focused on marine animals and insects. However, no study was reported in chelicerate. Scorpion chymotrypsin-like protease (SCP) was purified to homogeneity from delipidated hepatopancreases. The protease NH2-terminal sequence exhibited more than 60% monoacids identity with those of insect putative peptidases. The protease displayed no sequence homology with classical proteases. From this point of view, the protease recalls the case of the scorpion lipase which displayed no sequence homology with known lipases. The scorpion amylase purified and characterized by our time, has an amino-acids sequence similar to those of mammalian amylases. The enzyme was characterized with respect its biochemical properties: it was active on a chymotrypsin substrate and had an apparent molecular mass of 25 kDa, like the classically known chymotrypsins. The dependence of the SCP activity and stability on pH and temperature was similar to that of mammalian chymotrypsin proteases.
The solution structure and the disulfide pairings of a 36-residue proteinase inhibitor isolated from the insect Locusta migratoria have been determined using NMR spectroscopy and simulated annealing calculations. The peptide, termed PMP-C, was previously shown to inhibit bovine alpha-chymotrypsin as well as human leukocyte elastase, and was also found to block high-voltage-activated Ca2+ currents in rat sensory neurones. PMP-C has a prolate ellipsoid shape and adopts a tertiary fold hitherto unobserved in the large group of small canonical proteinase inhibitors. The over-all fold consists mainly of three strands arranged in a right-handed twisted, antiparallel, beta-sheet that demarcates a cavity, together with a linear amino-terminal segment oriented almost perpendicular to the three strands of the beta-sheet. Inside the cavity a phenyl ring constitutes the centre of a hydrophobic core. The proteinase binding loop is located in the carboxy-terminal part of the molecule, between two cysteine ...
Semantic Scholar extracted view of [The enhanced activity of chymotrypsin-like proteinases in the blood plasma of patients with hereditary hypercholesterolemia and the means for its correction]. by O. G. Ogloblina et al.
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Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
Results The authors identified 14 variants in CTRC, of which non-synonymous variants were detected in 71/584 CP patients (12.2%) and 22/598 controls (3.7%; OR 3.62, 95% CI 2.21 to 5.93; p=6.2×10−8). Rather than the commonly reported p.K247_R254del variant in Caucasians, p.V235I was the most common mutation in Indian CP patients (28/575 (4.9%); OR 7.60, 95% CI 2.52 to 25.71; p=1.01×10−5). Another pathogenic variant, p.A73T was identified in 3.1% (18/584) patients compared with 0.3% (2/598) in controls (OR=9.48, 95% CI 2.19 to 41.03, p=2.5×10−4). The authors also observed significant association for the synonymous variant c.180C,T (p.(=)) with CP (OR 2.71, 95% CI 1.79 to 4.12, p=5.3×10−7). Two novel nonsense mutations, p.G242AfsX9 and p.W113X were also identified exclusively in CP patients. No interaction between CTRC variants and p.N34S SPINK1 or p.L26V CTSB mutations was observed.. ...
Read Immobilization of proteolytic enzymes trypsin and α-chymotrypsin to cellulose matrix, Russian Journal of Applied Chemistry on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
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De Jersey J., Keough D.T., Stoops J.K. and Zerner B. (1974) A kinetic study of the deacylation of α benzamido trans cinnamoyl chymotrypsin: evidence for the intervention of non enzymic species. European Journal of Biochemistry, 42 1: 237-243. doi:10.1111/j.1432-1033.1974.tb03333.x ...
article{1e7da19b-137f-4fcf-9f74-7f6d6b4d2ece, abstract = {The loop region of chymotrypsin inhibitor 2 from barley has been employed as a scaffold for testing the intrinsic propensity of a peptide fragment to form a secondary structure. The helix formation of the nine amino acid residue segment Lys-Gln- Ala-Val- Asp- Asn- Ala-Tyr-Ala of helix E from subtilisin Carlsberg has been studied by the construction of a hybrid consisting of chymotrypsin inhibitor 2 (CI2) where part of the active loop has been replaced by the nonapeptide. An expression system for a truncated form of C12 where the 19 structureless residues of the N-terminus have been removed and Leu20 replaced,br/,,br, by methionyl was constructed from the entire 83-residue wild-type C12 gene by polymerase chain reaction,br/,,br, methodology. The gene encoding the hybrid was constructed from the truncated inhibitor gene. The stability of the truncated inhibitor and of the hybrid toward guanidinium chloride denaturation was examined. From ...
Intenzyme Forte™ is a broad spectrum proteolytic enzyme formulation, containing pancreatin, bromelain, papain, lipase, amylase, trypsin and alpha chymotrypsin. It may be utilized to support numerous protein metabolism pathways. Proteolytic enzymes are capable of exerting influence over a wide variety of physiological and biochemical processes. The benefits of Intenzyme Forte include its effect on muscle soreness and discomfort due to overexertion, the support of hormone processing, as well as providing support for healthy digestive, immune and circulatory functions.
A multi-digestive proteolytic enzyme formula, offering the profound health benefits of pancreatin, bromelain, papain, lipase, amylase, trypsin and alpha chymotrypsin, with the bioflavonoid boost of quercetin from rutin. Enzyme Ease® assists with inflammatory response in the body and supports the immune system when taken without food.* Taken with meals, it serves to support the digestive process.*. Proteolytic Enzyme Blend. ...
Delegates should have an improved understanding of the active substances within LDT secretions which contribute to these 3 clinical effects, with particular focus on the activity of trypsin and chymotrypsin on the wound bed; the broad-spectrum anti-microbial activity of LDT, including evidence of prevention and removal of biofilms; and the remodelling action of LDT secretions in vitro, including cell migration and neovascularisation ...
TY - JOUR. T1 - Proteolysis of the monomeric and dimeric C5b-9 complexes of complement. T2 - Alteration in the susceptibility to proteases of the C9 subunits associated with C5b-9 dimerization. AU - Yamamoto, K.. AU - Migita, S.. PY - 1981/1/1. Y1 - 1981/1/1. N2 - The C5b-9 monomer having the sedimentation coefficient of 23S was extracted from the rabbit erythrocyte membranes that had been treated with a limiting amount of C9-deficient human serum and of 125I-C9. Upon proteolysis by trypsin and chymotrypsin, the C9 subunits of this complex were cleaved by these enzymes at multiple sites, yielding fragments with m.w. ranging from 40,000 to 19,000. The uncomplexed C9 was also cleaved by both enzymes at multiple sites. By contrast, the C9 subunits of the C5b-9 dimer were found to be totally insusceptible to chymotrypsin under the conditions studied (37°C; 24 hr) and only partially susceptible to trypsin (33% of the C9 subunits were cleaved by trypsin into 2 fragments during incubation at 37°C for ...
I have received data from SPARC, Sick Kids Hospital Toronto, for the limited digest experiment I previously wrote about. This experiment aims to work out where the flexible linker regions of the protein structure are, therefore predicting which regions of the protein sequence correspond to folded domains.All of the experimental data is uploaded onto Zenodo.. Very similar proteolytically stable regions of huntingtin were mapped. despite limited cleavage of the protein with a different enzyme. This evidence further supports the domain mapping described previously.. I am now eagerly awaiting the insect cell construct test expression data, to see if we can make some of these putative domains recombinantly ...
Enzymes which are able to hydrolyze proteins. They are found in all living beings and are an important part of digestive enzymes: pancreatic (trypsin and chymotrypsin) and gastric (pepsin).. They are orally used for gastrointestinal disorders and topically on wounds and burns. Some (chymotrypsin) are used in cataract surgery. There is an increasing trend on type and therapeutic uses (Craik 2011). There is no evidence of its efficacy in the treatment of post-traumatic or post-surgical inflammations or in respiratory diseases. At latest update relevant published data on excretion into breast milk were not found. Because the small dose used and low plasma uptake of most topical dermatological and ophthalmological preparations it is unlikely that significant amounts of it will pass into breastmilk. Its high molecular weight turns further improbable any excretion into breastmilk. Due to its protein nature, when orally taken it is digested by the infants intestine, hence its absorption and passage
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In enzymes, as with other proteins, function is determined by structure. An enzyme can be a monomeric protein made up of about hundred amino acids or more, or an oligomeric protein consisting of several monomers, different or identical, that act together as a unit. As with any protein, each monomer is actually produced as a long, linear chain of amino acids, which folds in a particular fashion to produce a three-dimensional product. While it is well established that a proteins fold is determined by its primary structure, the factors that go into ensuring that the chain folds correctly and maintains its shape are complex, and still not completely understood, although general principles have been identified. Individual monomers may then combine via non-covalent interactions to form a multimeric protein. The final enzyme molecule might also be modified in various ways to make it active; for instance, chymotrypsin, a digestive protease, is produced in inactive form as chymotrypsinogen in the ...
Protease-Inhibitors. here fulfill a crucial role in regulating the life cycle of proteins, activating pro-enzymes or eliminating problematic proteins. In addition, proteases are secreted to process food, e.g. in the intestinal tract of animals. Protease Inhibitors used in protein purification procedures Whenever proteins are analyzed in biological samples or purified from a natural source, protease activity is a potential threat. During sample preparation, cells are frequently lysed and in this way they set free high amounts of protease activities that may digest the proteins of interest. The days of work for cell culture and protein sample preparation can be destroyed within a few seconds.Labs generally apply two basic strategies to knock out such unwanted proteolytic activities: (a) cooling the sample or cell lysate, and (b) adding chemical inhibitors of proteases. The most common proteases are the serine proteases Chymotrypsin, Kallikrein, Plasmin, Proteinase K, Thrombin and Trypsin. Hence ...
This gene encodes a member of a group of membrane-anchored chymotrypsin (S1)-like serine proteases. The enocoded protein is primarily expressed in the Leydig and Sertoli cells of the testis and may be involved in male fertility. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2010] ...
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利用液质联用研究重组水蛭素12肽与瑞替普酶融合蛋白(HV12p-rPA)的一级结构。采用基质辅助激光解析电离飞行时间质谱(MALDI-TOF-MS)测定水蛭素12肽与瑞替普酶融合蛋白(HV12p-rPA)的相对分子质量;采用液质联用分别分析HV12p-rPA的胰蛋白酶(trypsin)和胰凝乳蛋白酶(chymotrypsin)酶解产物。MALDI-TOF-MS测得HV12p-rPA的相对分子质量为41472 ...
2003: Highly Efficient Tight Fit Immobilization of .alpha.-Chymotrypsin in Mesoporous MCM-41: A Novel Approach Using Precursor Immobilization and ...
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