Recombinant Human Titin (TTN) Protein (His)

Name: Recombinant Human Titin (TTN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02328P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TTN.

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Product Overview

Description	Recombinant Human Titin (TTN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8WZ42
Target Symbol	TTN
Synonyms	MPRM; Cardiomyopathy dilated 1G (autosomal dominant); CMD1G; CMH 9; CMH9; CMPD 4; CMPD4; Connectin; DKFZp451N061; EOMFC; FLJ26020; FLJ26409; FLJ32040; FLJ34413; FLJ39564; FLJ43066; HMERF; LGMD2J; MU RMS 40.14; MYLK5; Rhabdomyosarcoma antigen; Rhabdomyosarcoma antigen MU RMS 40.14; Rhabdomyosarcoma antigen MU-RMS-40.14; Titin; TITIN_HUMAN; TMD; TTN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VFKCSVIGIPTPEVKWYKEYMCIEPDNIKYVISEEKGSHTLKIRNVCLSDSATYRCRAVNCVGEAICRGFLTMGDSEIFAVIAKKSKVTLSSLMEELVLKSNYTDSFFEFQVVEGPPRFIKGISDCYAPIGTAAYFQCLVRGSPRPTVYWYKDGKLVQGRRFTVEESGTGFHNLFITSLVKSDEGEYRCVATNKSGMAESFAALTLT
Expression Range	5398-5604aa
Protein Length	Partial of Isoform 6
Mol. Weight	26.5kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Protein kinase superfamily, CAMK Ser/Thr protein kinase family
Database References	HGNC: 12403 OMIM: 188840 KEGG: hsa:7273 STRING: 9606.ENSP00000343764 UniGene: PMID: 29386531 In a case-control study, there was a statistically significant association between an LOF variant in the TTN gene and early-onset AF, with the variant present in a small percentage of participants with early-onset AF (the case group). PMID: 30535219 novel titin gene-truncating mutation NM_001267550: p.Leu23499fs/c.70497_40498insT found in the proband as well as in her mother in woman with peripartum cardiomyopathy PMID: 29997384 Titin isoform expression differs in aortic stenosis and aortic regurgitation as adaptive response to different pathophysiologic scenarios. PMID: 29472025 TTN missense variants were commonly identified in arrhythmogenic cardiomyopathy patients in this cohort, but did not appear to play a primary role in ACM as causative variants. PMID: 29750433 This is the first study to suggest the involvement of the novel missense CACNA1C c.1786G>A and TTN c.49415G>A variants in the inheritance of symptomatic bradycardia and development of sick sinus syndrome. PMID: 29568937 We employed WES to detect the mutations of DCM patients and identified 2 novel mutations. Our study expands the spectrum of TTN mutations and offers accurate genetic testing information for DCM patients who are still clinically negative. PMID: 27544385 urinary concentration of titin correlated significantly with serum creatine kinase concentration, the best-known biomarker of Duchenne muscular dystrophy; the N-terminal fragment of titin in urine has potential as a diagnostic and clinical biomarker for DMD PMID: 29175173 we considered titin fragments as promising candidates for reliable and non-invasive biomarkers of muscle injury. PMID: 27991570 TTN plays a role in regulation of cardiac electrical conductance and coupling, and is a risk factor for cardiac arrhythmias and sudden cardiac death PMID: 27321809 The T-allele at rs10497520 in the TTN gene is associated with shorter skeletal muscle fascicle length and conveys an advantage for marathon running performance in habitually trained men. PMID: 28581678 An overview of the different neuromuscular disorders caused by mutations in the TTN gene, reviewing the molecular findings as well as the clinical data (review). PMID: 27854229 This review considers data on structural and functional features of titin, on the role of this protein in determination of mechanical properties of sarcomeres, and on specific features of regulation of the stiffness and elasticity of its molecules, and possible amyloid aggregation of this protein PMID: 29523065 Exome sequencing was conducted and a novel mutation c.107788T>C (p.W35930R) in the titin gene (TTN) was identified. PMID: 26392295 Study found that there is a missense mutation in the TTN gene, c.100126A > G (p.Thr33376Ala), in a family whose members suffer from familial dilated cardiomyopathy. TTN is closely related to dilated cardiomyopathy and is an important causative gene of familial dilated cardiomyopathy. PMID: 29109008 Truncating titin mutations cause a mild and treatable form of dilated cardiomyopathy. PMID: 27813223 Activation of titin protein represents an initial step forward adaptive remodelling of the exercised muscle and may also be involved in the initiation of myofibre repair. PMID: 28712031 Novel A178D missense mutation in titin is a cause of a highly penetrant familial cardiomyopathy with features of left ventricular noncompaction. PMID: 27625337 Quantitative models derived from large-scale human genetic and phenotypic data can be applied to truncating mutations in titin in dilated cardiomyopathy. PMID: 27625338 Variants near TTN and CCDC8 were associated with KI67 expression, and rs2288563 and rs2562832 in TTN are potential biomarkers for the prediction of clinical outcomes in hepatitis B-related hepatocellular carcinoma patients. PMID: 28700999 Recent studies classify pathogenic variants in the TTN gene as the main responsible for Familial Dilated Cardiomyopathy. PMID: 27736720 TTNtv might be a genetic modifier of HCM and confer an increased risk for cardiovascular death. PMID: 28822653 Heterozygous loss of RBM20 suffices to profoundly impair myocyte biomechanics by its disturbance of TTN splicing causing dilated cardiomyopathy. PMID: 27496873 Study identified a probable association between variation in TTN gene and patients with sudden unexpected death syndrome. PMID: 28704380 We report that missense variant in the A-band of TTN gene is the strongest candidate mutation for autosomal-dominant inguinal hernia with incomplete penetrance. PMID: 27115767 Titin-truncating variant is associated with dilated cardiomyopathy. PMID: 27869827 Data suggest that disulfide bonds can alter mechanical stability of proteins in different ways depending on properties of system. Disulfide-bonded E coli FimG (minor component of type 1 fimbriae) undergoes a 30% increase in its mechanical stability compared with its reduced counterpart. Unfolding force of human titan I91 domain exhibits decrease of 15% relative to the wild-type form. PMID: 28642368 TTN truncating variants were observed in nearly one fourth of young dilated cardiomyopathy patient population, in vast majority without conduction system disease. PMID: 28045975 detected an Linkage Disequilibrium block associated with a rapid functional decline in patients with sporadic ALS, which is linked to decreased expression of TTN. PMID: 26746183 An estimated probability of pathogenicity of TTN truncating mutations affecting all transcripts of TTN, identified in unselected dilated cardiomyopathy patients is 97.8%. PMID: 26777568 TTN variant segregated with hypertrophic cardiomyopathy in affected members of the family. PMID: 28223422 A distinct phenotype for patients with distal myopathy is associated with novel recessive TTN variants including a Serbian founder variant. PMID: 28295036 Results show that the titin I27Y9P variant has similar mechanical stability as the wildtype. PMID: 27021163 Phosphorylating Titin's Cardiac N2B Element by ERK2 or CaMKIIdelta Lowers the Single Molecule and Cardiac Muscle Force PMID: 26682816 Suggest a potential biological role for some TTN missense variants in dilated cardiomyopathy. PMID: 26567375 Data suggest that titin functions as an integrated protein chain where functionalities emerge from the joint action of titan and other sarcomere/A-band components (such as TCAP); titin exhibits tertiary elasticity and molecular shape memory. [REVIEW] PMID: 26517893 a large number of VUS in the TTN gene were identified from a cohort of samples from patients suffering cardiac diseases associated with sudden cardiac death. PMID: 26516846 TTN mutations have been strongly associated with four cardiomyopathies: Dilated cardiomyopathy, Hypertrophic cardiomyopathy, Arrhythmogenic right ventricular cardiomyopathy and Restrictive cardiomyopathy. PMID: 26024954 The distribution of truncating variants in a large series of women with peripartum cardiomyopathy was remarkably similar to that found in patients with idiopathic dilated cardiomyopathy. PMID: 26735901 Cleavage of C-terminal titin by CAPN3 is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy. PMID: 25877298 findings indicate that titin mutations cause dilated cardiomyopathy by disrupting critical linkages between sarcomerogenesis and adaptive remodeling PMID: 26315439 Engineered all four of the naturally occurring human M10 (the extreme C-terminus of titin) missense mutants and biophysically characterized them in vitro. PMID: 25739468 an increase in intracellular Ca(2+) concentration leads to Ca(2+) binding to the PEVK region of titin. PMID: 25421125 An increase in the degree of titin phosphorylation results in increased proteolytic degradation of this protein, that contributes to the development of skeletal muscle atrophy. PMID: 26394485 TTNtv is the most common genetic cause of dilated cardiomyopathy in ambulant patients PMID: 25589632 MMP-2 degraded Titin fragment in serum is related to induction of skeletal muscle atrophy. PMID: 25077715 individual subfragments of titin and myomesin composed of Fn type III and Ig-like domains can activate expression of two IGF-1 splice forms in cultured myoblasts PMID: 25152160 Patients with hypertension and heart failure with preserved ejection fraction had an increase in S11878(S26), no change in S12022(S170) and a decrease in S4185(S469). There were no significant differences between HTN(-)HFpEF or controls at these 3 sites. PMID: 25637629 Results suggest that mutation in TTN could be implicated in the pathogenesis of puerperal cardiomyopathies. PMID: 24558114 this study presents here the X-ray structure of the human titin:obscurin M10:O1 complex extending our previous work on the M10:OL1 interaction. PMID: 25490259

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Human Titin (TTN) Protein (His)

Recombinant Human Titin (TTN) Protein (His)

Product Overview

Target Details

FAQs