Recombinant Human Talin-1 (TLN1) Protein (GST)

Name: Recombinant Human Talin-1 (TLN1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03643P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Talin-1 (TLN1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y490
Target Symbol	TLN1
Synonyms	ILWEQ; Talin 1; Talin; Talin-1; TLN 1; TLN; Tln1; TLN1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDII
Expression Range	92-399aa
Protein Length	Partial
Mol. Weight	62.8kDa
Research Area	Signal Transduction
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	Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
Subcellular Location	Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell surface. Cell junction, focal adhesion.
Database References	HGNC: 11845 OMIM: 186745 KEGG: hsa:7094 STRING: 9606.ENSP00000316029 UniGene: PMID: 29936723 Calpain small subunit 1 (Capn4) overexpression increased the protein level of cleaved talin and and activated the focal adhesion kinase (FAK)/AKT/MAPK signaling in 786-O cells, while Capn4 silencing decreased the protein level of cleaved talin in Caki-1 cells. PMID: 29648579 Talin-1 induces proliferation and migration of vascular smooth muscle cells obtained from patients with thoracic aortic dissection. PMID: 28637452 Here, the authors show that cortical microtubule stabilization sites containing CLASPs, KIF21A, LL5beta and liprins are recruited to focal adhesions by the adaptor protein KANK1, which directly interacts with the major adhesion component, talin. Structural studies showed that the conserved KN domain in KANK1 binds to the talin rod domain R7. PMID: 27410476 Vinculin head-tail interaction is required on soft substrates to destabilize vinculin and talin in FAs, and to allow hMSCs branching. Another module involves paxillin and FAK, which soft substrates also destabilize, but independently of vinculin head-tail interaction. This multi-modularity may be key to allow a versatile response to complex biomechanical cues. PMID: 27169142 The central role of talin and vinculin in cell adhesions suggests that the disintegration of the tissue in atherosclerosis could be partially driven by downregulation of these genes, leading to loosening of cell-ECM interactions and remodeling of the tissue. PMID: 27816808 Application of these techniques to new talin biosensors reveals an intramolecular tension gradient across talin-1 that is established upon integrin-mediated cell adhesion. The tension gradient is actomyosin- and vinculin-dependent and sensitive to the rigidity of the extracellular environment PMID: 28945706 Our findings confirm the role of Talin-1 in carcinogenesis and provided a set of novel therapeutic targets for the treatment of hepatocellular carcinoma PMID: 28099903 These data show that TLN1 can act as a viral restriction factor that suppresses hepatitis B virus replication, and suggest that the HBx relieves this restriction by inducing TLN1 degradation. PMID: 27775586 The ERK pathway was responsible for these promoting effects of Talin1 knockdown in HCC cells. PMID: 28375585 This study showed that serum sTalin-1 levels were associated with a sustained increase in disability after MS attack but not with serum anti-Talin-1 antibody levels. PMID: 28284333 The Rap1-RIAM-talin axis of integrin activation and blood cell function PMID: 27207789 These findings suggested that Talin-1 protein was significantly upregulated in PCa tissues compared with that of BPH tissue and Talin-1 expression was an independent predictor for lymph node metastasis and biochemical recurrence of PCa. PMID: 27442684 Serum talin-1 had 97.7% sensitivity. PMID: 27644664 Both TLN-1 and TLN-2 levels correlate with tumorigenicity in human HCC, indicating that these molecules constitute important molecular targets for the diagnosis and/or treatment of hepatocellular carcinoma . PMID: 26822056 TLN1 significantly increases in refractory glioblastoma multiforme PMID: 26336988 Applying correlative imaging to link live cell and fixed immunofluorescence data on a single cell basis, we related per cell talin-1 levels to per cell measures quantitatively defining an array of cellular properties. PMID: 26000342 Disruption of the RIAM/lamellipodin-integrin-talin complex markedly impairs cell migration. PMID: 26419705 Our data demonstrate that high expression of Talin-1 is associated with significantly poorer OS and poorer DMFS in NPC and depletion of Talin-1 expression inhibited NPC cell migration and invasion. Talin-1 may serve as novel prognostic biomarker in NPC. PMID: 25925041 results identify talin as the primary determinant of FA nanoscale organization and suggest how multiple cellular forces may be integrated at adhesion sites PMID: 26283369 The activation of vinculin by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin association. PMID: 24452080 Talin extension is a key step in sensing and responding to substrate stiffness at cell adhesion sites. PMID: 25142525 Data (including data from molecular dynamic simulations) suggest specific interactions between glycoprotein GPIIb/GPIIIa complex transmembrane/C-terminal domains and talin-1 in cell membrane environment during platelet activation. PMID: 24677266 phosphorylation of talin1 leading to beta1 integrin activation is a novel mechanism that increases metastatic potential of prostate cancer cells. PMID: 24793790 Data suggest that anionic lipids (such as phosphatidylinositol phosphates) play crucial role in localization of peripheral membrane proteins (such as TLN1, auxilin-1, and PTEN [phosphatase and tensin homolog]). [review-like article] PMID: 25233425 Low levels of Talin-1 expression are correlated with increased invasion and migration in liver cancer. PMID: 24761880 Data indicate the role of vinculin in inducing the talin mediated integrin activation. PMID: 24446374 MMP-2 regulates human platelet activation through hydrolysis of talin PMID: 24136115 Talin has a role in regulating moesin-NHE-1 recruitment to invadopodia in breast cancer PMID: 24891603 miR-9 plays a role as a tumor suppressor in OSC by suppressing TLN1 expression. PMID: 23722670 These results indicate that mechanical forces loaded to focal adhesions (FAs) facilitate vinculin binding to talin at FAs. PMID: 24452377 High Serum talin-1 expression is associated with hepatocellular carcinoma. PMID: 23886189 Data indicate that KIF14 and TLN1 loss-of-function significantly enhanced chemosensitivity in four triple-negative breast cancer (TNBC) cell lines. PMID: 23479679 Talin1 has unique expression versus talin 2 in the heart and modifies the hypertrophic response to pressure overload. PMID: 23266827 CtsH-mediated processing of talin might promote cancer cell progression by affecting integrin alphaVbeta3 activation and adhesion strength PMID: 23204516 Agonist stimulation, talin-1, and kindlin-3 are crucial for alpha(IIb)beta(3) activation in a human megakaryoblastic cell line, CMK. PMID: 23022222 Kindlin-2 and talin head do not interact with one another but can bind simultaneously to the integrin beta(3) tail without enhancing or inhibiting the interaction of the other binding partner. PMID: 22648415 Low Talin1 is associated with hepatocelluar carcinoma. PMID: 22471464 Talin1 is required for inside-out activation of integrin beta1 during Bartonella henselae infection. PMID: 22045736 FAK promotes talin recruitment to nascent adhesions occurring independently of talin binding to beta1 integrins. PMID: 22270917 Talin1 is required for contact-dependent CD4-positive T cell proliferation in talin1 transgenic mice. Talin1 is not required for contact-independent CD4+ T cell proliferation. PMID: 22075696 We investigated the role of talin-1, kindlin-3, and alpha-actinin-1 in the upregulation of alpha(4)beta(1) integrin affinity and consequent inflammatory leukocyte adhesive events PMID: 21911599 Talin-1 upregulation is associated with disease progression in hepatocellular carcinoma. Thus, it may serve as a prognostic marker. PMID: 21846996 Adhesions within the carcinoma matrix create a matrix environment in which exposure to cisplatin induces proliferation through the function of integrin beta, talin and FAK pathways that regulate NF-kB nuclear activity. PMID: 21720550 Talin-1 and vinculin negatively affect tyrosine phosphorylation of paxillin, a novel positive regulator of HIV-1 infection, and impose an early block to infection by distinct retroviruses. PMID: 21763488 We show that sequential cleavage of C-terminal amino acids from the beta(2) cytoplasmic tail of LFA-1, by CatX, enhances binding of the adaptor protein talin to LFA-1 and triggers formation of the latter's high-affinity form PMID: 21454358 This review discusses the general function of talin 1 and talin 2, as well as vinculin/metavinulin, with emphasis on what is understood about their role in the cardiac myocyte and in whole heart. PMID: 19952892 Studies suggest that the perturbed orientation of talin relative to the membrane in the F2 mutant would be expected to in turn perturb talin/integrin interactions. PMID: 20947017 Data from talin crystal structure reveal a novel FERM domain with a linear domain arrangement, plus an additional domain F0 packed against F1. PMID: 20947018 Rap1-mediated activation of alpha(M)beta(2) in macrophages shares both common and distinct features from Rap1 activation of alpha(IIb)beta(3) expressed in CHO cells. PMID: 20665668

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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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