Recombinant Human Desmin Protein (N-6His)

Name: Recombinant Human Desmin Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0830NP
Availability: InStock

BL-0830NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Desmin is produced by our E.coli expression system and the target gene encoding Val261-Leu470 is expressed with a 6His tag at the N-terminus.
Accession	P17661
Synonym	Desmin; DES
Gene Background	Desmin is a cytoplasmic protein and belongs to the intermediate filament family. interacts with DST and MTM1. Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. Desmin is the main intermediate filament in mature skeletal, cardiac and smooth-muscle cells. DES founctions as homopolymers to form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. .Defects in DES are cause of the myopathy myofibrillar type 1, cardiomyopathy dilated type 1I, and neurogenic scapuloperoneal syndrome Kaeser type.
Molecular Mass	26.7 KDa
Apmol Mass	30 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin.
Subcellular Location	Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm. Cell membrane, sarcolemma. Nucleus.
Protein Families	Intermediate filament family
Database References	HGNC: 2770 OMIM: 125660 KEGG: hsa:1674 STRING: 9606.ENSP00000363071 UniGene: PMID: 28171858 Desmin, Glial Fibrillary Acidic Protein, Vimentin, and Peripherin are type III intermediate filaments that have roles in health and disease [review] PMID: 29196434 Phenotypic expression of a novel desmin gene mutation: hypertrophic cardiomyopathy followed by systemic myopathy. PMID: 29167554 Targeted sequencing revealed trigenic mutations: c.700G>A/p.E234K in DES, c.2966G>A/p.R989H in MYPN, and c.5918G>C/p.R1973P in CACNA1C in a family of hypertrophic cardiomyopathy with early repolarization and short QT syndrome. PMID: 28427417 demonstrate that the expression of mutant desmin causes disruption of the extrasarcomeric desmin cytoskeleton and extensive mitochondrial abnormalities regarding subcellular distribution, number and shape PMID: 27393313 Mutation in the Core Structure of Desmin Intermediate Filaments Affects Myoblast Elasticity PMID: 28793217 Data show that the filament elongation of both desmin and keratin K8/K18 proceeds very similar to that of vimentin. PMID: 27304995 Cdk1-induced desmin phosphorylation is required for efficient separation of desmin-IFs and generally detected in muscular mitotic cells in vivo. PMID: 27565725 Desmin, Lamin A/C, MMP9, and histone H4 were upregulated in the placental villi of women experiencing early pregnancy loss. PMID: 26947931 Ile367Phe, Pro419Ser, and Arg415Glu mutations were associated with desminopathy causing cardiomyopathy in 4 families studied. PMID: 26431784 Increasing desmin abnormalities were correlated with diastolic dysfunction progression. PMID: 25732530 expression level of mutant versus wild-type desmin in mouse model as well as in skeletal muscle specimens derived from human R350P desminopathies; findings demonstrate missense-mutant desmin inflicts changes of the subcellular localization and turnover of desmin itself and of direct desmin-binding partners PMID: 25394388 Results propose that the mutations affect desmin structure and cause its aberrant folding and subsequent aggregation, triggering disruption of myofibrils organization. PMID: 25541946 identified disruption of the desmin system in gastrocnemius myofibers as an index of the myopathy and limitation of muscle function in patients with peripheral artery disease. PMID: 25575565 The desmin intermediate filament network plays a major role in striated muscle development and maintenance by integrating and coordinating most cellular components necessary for proper mechanochemical signaling, organelle cross-talk, energy production and trafficking processes required for proper tissue homeostasis. [Review] PMID: 25680090 Data suggest that loss of the desmin-p. A120D filament localization at the intercalated disk indicates its clinical arrhythmogenic potential. PMID: 24200904 we describe a new mutation located in the coiled 1B domain of desmin and associated with a predominant cardiac involvement and a high degree of cardiac sudden death in a large Indian pedigree with 12 affected members PMID: 24441330 Perfomed proteomic analysis on a transgenic mouse model of severe cardiac hypertrophy; compared data to dataset of heart failure found MYH7, IGFBP7, ANXA2, and DESM to be biomarker candidates for heart failure. PMID: 23713052 autosomal recessive mutations in DES cause LGMD2 phenotype without features of myofibrillar myopathy. PMID: 23687351 Data suggest that for some filament-forming desmin mutants, the molecular etiology of desminopathy results from subtle deficiencies in their association with nebulin, a major actin-binding filament protein of striated muscle. PMID: 23615443 Sequencing of the desmin gene showed a splice-site mutation (IVS3+1G-->A), which was absent in 300 healthy control subjects. PMID: 22484823 Phenotypic features in patients with desmin tail domain mutations are similar to those in patients with mutations localized in the 1B and 2B alpha-helical domains. PMID: 23051780 The results of this study indicate that atrioventricular conduction block without cardiac structural abnormalities may be an intrinsic feature of disease associated with specific desmin mutation PMID: 23036309 in the absence of skeletal muscle involvement suggestive of a desminopathy, the probability of DES mutations in ARVC is very low. These findings have important implications in the mutation screening strategy for patients with ARVC. PMID: 23168288 The results of this study indicated that no cases showed missense mutations in the Desmin. PMID: 22349865 Data show that calretinin and CK5/6 were positive in 100 and 64% of mesotheliomas, and 92 and 31% of reactive effusions, respectively, and desmin was negative in all malignant cases and positive in 85% of reactive effusions. PMID: 23075894 A heterozygous C-to-T mutation in the desmin gene on chromosome 2q35 caused autosomal dominant myofibrillar myopathy with arrhythmogenic right ventricular cardiomyopathy 7 in a Swedish family. PMID: 22395865 Frequent desmin (32%) and occasional CD34 (6%) expression are encountered in cellular fibrous histiocytoma. PMID: 22775584 Data indicate that the interaction and co-localization of mutant and wild-type desmin proves the co-existence of heterogeneous filaments in living cells. PMID: 22403400 analysis of CD105, CD31, alpha-SMA, vimentin and desmin expression on a series of normal human heart tissues varying between five and 33 weeks PMID: 22395512 This study demonistrated that Patients carrying DES mutations presenting with myofibrillar myopathies or without muscle involvement, are at high risk of developing major cardiac complications. PMID: 22153487 the expression of mutant desmin leads to increased mechanical stiffness, which results in excessive mechanical stress in response to strain and consecutively to increased mechanical vulnerability and damage of muscle cells. PMID: 22386993 Ankrd1 and desmin may play important roles in airway smooth muscle cell homeostasis. PMID: 22085644 49 mutations have been identified in the desmin gene, which alter the desmin filament assembly process through different molecular mechanisms and also its interaction with its protein partners. Review. PMID: 21982405 these studies highlight the importance of desmin in maintaining cardiomyocyte structure and illustrate how disrupting this network can be deleterious to the heart--{REVIEW} PMID: 21784990 study of patients with heart dilation of various origins; conclude A213V desmin substitution represents a rare polymorphism that plays role as predisposing factor resulting in maladaptive heart remodelling in presence of other pathological factors PMID: 21842594 Novel mutations of desmin gene were linked with cardiomyopathy in patients from 5 Chinese families with desminopathy. PMID: 20654101 Six novel mutations and one previously reported mutation in the desmin gene were identified in the patients PMID: 20696008 the state of desmin-filament assembly is crucial for synemin anchorage and consequently might involve mechanical and functional stability of the cytoskeletal network PMID: 21262226 study provides evidence on functional consequences of a novel mutation, N116S, identified in the desmin 1A segment of the rod domain for the development of arrhythmogenic right ventricular cardiomyopathy PMID: 20829228 Case Report: present a rare case of desmin-related hypertrophic cardiomyopathy. Cardiac magnetic resonance imaging revealed fibrosis in the lateral wall of the left ventricle. PMID: 21083940 mutations in MTM1 disrupted the MTM1-desmin complex, resulting in abnormal intermediate filament assembly and architecture in muscle cells PMID: 21135508 Desmin mutations affects the localization of desmoplakin and plakophilin-2 at the intercalated disk suggesting a link between desmosomal cardiomyopathies (mainly affecting the right ventricle) and cardiomyopathies caused by desmin mutations. PMID: 20423733 study of aggregation properties of desmin in vitro & aggregation state of desmin in homogenates of transfected cells; detected divergent assembly patterns for 3 different desmin missense mutations PMID: 20448486 The Uruguayan family with severe cardiomyopathy carries an unusual deletion p.E114del within the 1A rod domain of desmin. PMID: 20133133 the "tail" domain is responsible for attractive filament-filament interactions PMID: 20171226 The "head" mutations in desmin proteins impacting on intermediate filament assembly properties and their competition for binding to cellular anchoring structures might explain part of the molecular mechanism that causes myhofibrillar myopathy disease. PMID: 19763525 A localized effect of desmin on the structure of the cardiac intercalated disks might contribute to disease pathogenesis PMID: 19879535 Data showed that the elevated expression of desmin was correlated with the severity and differentiation of CRC. PMID: 19460759 structural and functional analysis of a new variant causing desmin-related myopathy PMID: 11668632

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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