Recombinant Human Claudin-11 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1292

Recombinant Human Claudin-11 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1292
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Product Overview

Tag Fc
Host Species Human
Accession O75508
Synonym OSP, OTM
Background Claudin-11, also known as CLDN11, belongs to the group of claudins. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands function as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions.Claudin-11 is a tight junction associated protein and is a major component of central nervous system (CNS) myelin that is necessary for normal CNS function. Human blood-testis barrier disruption is related to a dysfunction of CLDN11 gene. It plays an important role in regulating proliferation and migration of oligodendrocytes.
Description A DNA sequence encoding the human CLDN11 (O75508) (Val23-Arg82) was expressed with the Fc region of mouse IgG1 at the N-terminus.
Source HEK293
Predicted N Terminal Asp
AA Sequence Val23-Arg82
Molecular Weight The recombinant human CLDN11/mFc comprises 296 a.a. and has a predicted molecular mass of 33.2 kDa. The apparent molecular mass of the monomer is approximately 37 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Protein Families Claudin family
Database References

Gene Functions References

  1. expression of claudin-11 in cutaneous squamous cell carcinoma (cSCC) cells depended on the activity of p38delta MAPK; knock-down of claudin-11 enhanced cSCC cell invasion PMID: 27992079
  2. Authors demonstrated that CLDN11 promoter hypermethylation is a frequent event in LSCC, and contributes to metastasis and progression of LSCC. PMID: 28743857
  3. The expression of claudin-11, -23 was remarkably downregulated in gastric cancer. PMID: 28350854
  4. Claudin-11 might represent the essential component of the blood-testis barrier in human. PMID: 27486954
  5. the expression of miR-99b was inversely correlated with CLDN11 levels . These findings suggest that a high level of miR-99b expression is an independent prognostic factor and correlates with poor survival of patients with Hepatocellular carcinoma (HCC) PMID: 26134929
  6. CLDN11 is an epigenetic biomarker for malignancy in dysplastic nevus and melanoma. PMID: 24999589
  7. these data suggest that cancer cells may induce CLDN11 overexpression and subsequent collective migration of peritumoral CAFs via TGF-beta secretion. PMID: 24268521
  8. The expression of claudin-11 was up regulated in gastric cancer tissue. PMID: 23919729
  9. The spatial organization of claudin-11 and connexin-43 is altered in men with primary seminiferous tubule failure. PMID: 23706332
  10. disorganization of claudin-11 expression in Sertoli cells might be one of the factors involved in the impairment of spermatogenesis. PMID: 22951003
  11. Treatment with 3-deazaneplanocin A, an inhibitor of H3K27 methyltransferase, attenuated CLDN11 induction by serum stimulation in parallel with sustained miR-1275 expression PMID: 22736761
  12. claudin-11 may have a role in preventing cancer progression and may serve as a therapeutic target in reducing metastasis PMID: 21468549
  13. late spermatogenic wave may negatively regulate claudin-11 gene activation and the subcellular localization of claudin-11 in Sertoli cells, thus altering the blood testis barrier in the human testis PMID: 20850723
  14. Claudins 11,expression in meningiomas. PMID: 20546350
  15. hypermethylation of CLDN11, leading to downregulated expression, contributes to gastric carcinogenesis by increasing cellular motility and invasiveness PMID: 19956721
  16. Contribution of the tight junction protein CLDN11 to barrier function in endothelial cells is novel and may reflect hemodynamic requirements of the corpus cavernosum. PMID: 19622796
  17. Data demonstrate that in rhesus monkeys immune responses directed at human OSP are encephalitogenic, leading to inflammatory responses throughout the central nervous system and to selective demyelination of the optic nerve. PMID: 18412169
  18. the disruption of the blood-testis barrier is related to a dysfunction of claudin-11 and not to a failure of its expression. PMID: 19241088

FAQs

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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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