Recombinant Human S100A11 Protein

Name: Recombinant Human S100A11 Protein
Brand: Beta LifeScience
SKU: BL-1964NP
Availability: InStock

BL-1964NP: 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 Protein S100-A11 is produced by our E.coli expression system and the target gene encoding Met1-Thr105 is expressed.
Accession	P31949
Synonym	Protein S100-A11; Calgizzarin; Metastatic lymph node gene 70 protein; MLN 70; S100A11; Protein S100-C; S100 calcium-binding protein A11; MLN70; S100C
Gene Background	S100A11 is a member of the S100 family of calcium binding proteins. Human S100A11 contains two EF hand motifs and shares 82% amino acid sequence identity with mouse and rat S100A11. It forms covalent homodimers upon transglutamination and also disulfide-linked tetramers. S100A11 is secreted by keratinocytes and can be crosslinked into the cornified envelope of the skin. Dimerization enhances its ability to signal through RAGE on keratinocytes, induce the production of EGF family proteins, and induce cell proliferation. Dimerization also enables S100A11 to bind RAGE on chondrocytes, leading to chondrocyte hypertrophy and catabolism of the cartilage matrix. S100A11 is additionally found in the cytosol where it becomes phosphorylated and translocates to the nucleus in response to DNA damage, RELM alpha exposure, or elevated extracellular calcium concentrations. Calcium also promotes S100A11 association with S100B as well as Annexins A1, A2, and A6. S100A11-Annexin A2 complexes are recruited to sites of plasma membrane damage where they facilitate membrane repair in migrating cancer cells. S100A11 is upregulated in various cancers and supports tumor cell proliferation, invasion, and migration. In addition, S100A11 is produced in the ovary, and it acts on cumulus cells to inhibit oocyte fertilization.
Molecular Mass	11.7 KDa
Apmol Mass	12 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, 1mM DTT, 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	Facilitates the differentiation and the cornification of keratinocytes.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	S-100 family
Database References	HGNC: 10488 OMIM: 603114 KEGG: hsa:6282 STRING: 9606.ENSP00000271638 UniGene: PMID: 29569474 Results show that S100A11 expression is up-regulated by BC200 through stabilizing its mRNA and that S100A11 critically mediates the ability of BC200 RNA to induce cancer cell migration and invasion. PMID: 28277927 identified as a new regulator of Aldo-induced collagen production in human cardiac fibroblasts. PMID: 28739510 Furthermore, we identify flotillin-1 (FLOT1) and histone H1 as downstream factors for cytoplasmic and nuclear pathway of S100A11, which are required for LASP1-S100A11 axis-mediated epithelial-mesenchymal transition and colorectal cancer progression. PMID: 27181092 In patients with rheumatoid arthritis, S100A11 is up-regulated and is associated with inflammation and disease activity. PMID: 28446208 S100A11 overexpression correlates with an aggressive malignant phenotype and may constitute a novel prognostic factor for HGSC PMID: 26574635 we studied S100A11 and noted knockdown of S100A11 using short hairpin RNA, which inhibited proliferation, invasion, and migration of renal carcinoma cells as well as increased expression of E-cadherin and decreased expression of epidermal growth factor receptor/Akt in renal carcinoma cells. Therefore, S100A11 may be a key molecular target for treating renal carcinoma. PMID: 28513300 higher S100A11 expression was associated with statistically significant decrease in disease-free survival in clear cell renal cell carcinoma PMID: 26472670 the up-regulation of S100A11 plays a role in tumor progression, particularly in KRAS-mutated lung adenocarcinomas PMID: 26544866 metastatic cancer cells have elevated rate of cell injury and they rely on the S100A11-ANXA2 complex to enable cell membrane repair. S100A11 in a complex with Annexin A2 helps reseal the plasma membrane. PMID: 24806074 All three markers correlated significantly with regional lymph node metastasis: FXYD3 (p = 0.0110), S100A11 (p = 0.0071), and GSTM3 (p = 0.0173) in colon cancer lymphatic metastasis. PMID: 22430872 The EGFRvIII-STAT3 pathway promotes cell migration and invasion by upregulating S100A11 in hepatocellular carcinoma. PMID: 24376686 Proteomic data suggest a limited protein set is involved in SET- (template activating factor-I-) mediated cytotoxicity of TCE (trichloroethylene) in hepatocytes; this set includes CFL1 (cofilin 1), PRDX2 (peroxiredoxin 2), and S100-A11 (calgizzarin). PMID: 24631019 Our data indicate that S100A11 overexpression exerts a protumoral functional role in papillary thyroid carcinoma pathogenesis. PMID: 23928665 Data suggest that S100A11 is involved in maintenance of p21-CIP1 (cyclin-dependent kinase inhibitor 1A) protein stability (up-regulation; down-regulation) and appears to function as inhibitor of apoptosis in keratinocytes. PMID: 23745637 the structure of human calcium-bound S100A11. PMID: 22903637 Endometrial S100A11 is a crucial intermediator in EGF-stimulated embryo adhesion, endometrium receptivity, and immunotolerance via affecting Ca2+ uptake and release from intracellular Ca2+ stores. PMID: 22869607 Using transcriptional signatures of blood samples,identified S100A11 as a potential diagnostic marker of infective endocarditis, and AQP9 as a potential prognostic factor. PMID: 22319637 The expression level of S100C in lung cancer tissue was lower than that in ambient tissue. PMID: 18589612 investigated S100A11 expression in various subtypes of lung cancer and explored its role in cell proliferation. PMID: 21861103 S100A11 mediates HIMF-induced smooth muscle cell migration, vesicular exocytosis, and nuclear activation. PMID: 21139050 Data support that S100A11 is a novel diagnostic marker in breast carcinoma. PMID: 20372844 S100C is a new tumor marker protein, the expression of which significantly decreases after malignant transformation of human tissues. PMID: 11873942 S100Cis a key mediator of the Ca(2+)-induced growth inhibition of human keratinocytes in culture, and may be mediate growth regulation in vivo as well. PMID: 14623863 that redistribution along microtubules is a mechanism whereby S100A11 is positioned at the cell periphery in preparation for transglutaminase-dependent crosslinking. PMID: 14962086 Up-regulation of S100A11 was associated with the development of lymph node metastases in gastric cancer PMID: 15138568 Of several tested, only an N-terminal peptide with 19 amino acid residues induces apoptosis in human keratinocyte and squamous-cell carcinoma cell lines PMID: 15241500 findings suggest that S100A11 has an anti-apoptotic function and is related to the process of growth of human uterine leiomyoma PMID: 15322223 Down-regulation of S100C is associated with bladder cancer progression PMID: 15701847 Expression of S100A11, a putative tumor suppressor gene, is increased in the early stage of pancreatic carcinogenesis and decreased during subsequent progression to cancer. PMID: 17000675 S100C/A11-mediated pathway is at least partly involved in conferring upon human squamous cell cancers resistant to TGFbeta-induced growth suppression PMID: 17476473 The results indicated that the upregulation of S100A11 expression in non-small cell lung cancer tissues was significantly associated with higher tumor-node-metastasis stage (P = 0.001) and positive lymph node status PMID: 17537172 Proteomic mapping using a selective subcellular extraction kit revealed S100A11 as a new member of the S100 protein family modulated by glucocorticoids in keratinocytes. PMID: 17624315 Ca(2+)-dependent binding of S100A11 to ANXA1 facilitated the binding of the latter to cPLA(2), resulting in inhibition of cPLA(2) activity PMID: 17932043 These findings indicate that S100A11 plays a dual role in growth regulation of epithelial cells. PMID: 17978094 These findings suggest S100A11 could be helpful in the pathological study of colorectal cancer, especially for the classification of different stages in colorectal cancer. PMID: 18340452 S100/A11 and p21 gene expression was also found to be significantly lower in acute and chronic atopic dermatitis skin. PMID: 18385759 S100A11 targets Rad54B to sites of DNA DSB repair sites and has a role in p21-based regulation of cell cycle PMID: 18463164 Following transformation by transglutaminase 2, S100A11 acquires the capacity to signal through the p38 MAP kinase pathway, accelerate chondrocyte hypertrophy, and couple inflammation with chondrocyte activation to promote progression of osteoarthritis. PMID: 18523305 Phosphorylation of S100A11 induces a structural perturbation in the N-terminal edge of helix 1 and enables the phosphoryl group to be exposed to the solvent, allowing it to be recognized by the binding partner, nucleolin. PMID: 18618420 S100A11 differentially expressed in primary hepatocellular carcinoma , primary colorectal, and liver PMID: 19048101 Inhibition of S100A11 gene expression impairs the ability of keratinocytes to control vaccinia virus replication via downregulation of IFN-lambda receptor IL-10R2. PMID: 19577285 Down-regulation of S100C expression is associated with increasing tumor aggressiveness and poor prognosis in bladder cancer patients. PMID: 15701847

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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.