Recombinant Human S100A4 Protein

Name: Recombinant Human S100A4 Protein
Brand: Beta LifeScience
SKU: BL-1698SG
Availability: InStock

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Product Overview

Tag	N/A
Host Species	Human
Accession	P26447
Synonym	Protein S100-A4, Calvasculin, Metastasin, Placental calcium-binding protein, Protein Mts1, S100 calcium-binding protein A4, CAPL, MTS1 , Recombinant Human S100 Calcium Binding Protein A4 (S100A4)
Background	S100A4 is a calcium-binding protein related to the S100 family of proteins. It is known also as a growth-related protein, CAPL. It is expressed at high levels in different mouse metastatic cells and in normal tissues (thymus, spleen) and activated macrophages, T cells, neutrophils, monocytes, macrophages.
Description	Recombinant Human S100A4 was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	12.0 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human S100A4 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9. Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis. Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels. Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes. In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors.
Subcellular Location	Secreted. Nucleus. Cytoplasm.
Protein Families	S-100 family
Database References	HGNC: 10494 OMIM: 114210 KEGG: hsa:6275 STRING: 9606.ENSP00000346294 UniGene: PMID: 29901152 S100A4 expression is induced by the TGF-beta pathway,. PMID: 29141874 This meta-analysis showed that overexpression of S100A4 seems to be associated with tumor progression and poor prognosis of PC patients. PMID: 29578167 clusterin promotes growth and invasion in renal cell carcinoma cells in vitro and in vivo through upregulation of S100A4 PMID: 29400663 miR-3189-3p mimics enhanced the effects of the S100A4 siRNA on the inhibition of gastric cancer cell proliferation and migration by targeting CFL2. PMID: 29342841 Urine S100A4 shows the most promise as an lupus nephritis (LN) activity biomarker. PMID: 29065913 S100A4 is up-regulated in cervical adenocarcinomas and squamous cell carcinomas. PMID: 28921916 Network analysis of overlapping genes revealed the effects on tubulins (Tubb2a, Tubb3, Tubb4b), Nfe2l2, S100a4, Cd44, and Nfkb2, all of which are linked to TBI-relevant outcomes, including epileptogenesis and tissue repair PMID: 27530814 Authors first provide experimental evidence suggesting that FAM107B was downregulated by S100A4 in gastric cancer MGC803 cells. And FAM107B at least partially mediates the biological effect of S100A4 in the cells. PMID: 28675500 MiR-187 could interact with S100A4 3'-UTR. PMID: 29303365 Both the calcium-binding ability and the C-terminal region of S100A4 are important for cancer initiatin cells to sustain their stemness properties and malignancy in head and neck cancers. PMID: 27793047 Studied the role and expression of MIR296 in the metastasis and epithelial-mesenchymal transition of colorectal cancer. Found MIR296 inhibited migration and invasion of tumor cells, as well as suppressed S100A4 abundance in tumor cells. PMID: 28209128 S100A4-expression was associated with poor outcome in early-stage breast cancer, but the low percentage of positive tumors and the modest survival differences imply that the clinical utility in selection of patients for adjuvant treatment is limited. PMID: 28058579 The relative expression of S100A4 mRNA was higher when mod-SHEM was used, although significant differences were detected only when the expression levels were compared with those found in LPCs incubated with IOBA-FBS PMID: 27911610 High S100A4 expression is associated with Mesenchymal Transition in Glioblastoma. PMID: 28807938 our findings demonstrate that S100A4 is post-transcriptionally regulated by tumor suppressor microRNAs PMID: 28423501 findings indicate that Idiopathic pulmonary fibrosis mesenchymal progenitor cells are intrinsically fibrogenic and that S100A4 confers mesenchymal progenitor cells with fibrogenicity. PMID: 28530639 S100a4 is expressed in a limited number of stromal cells throughout the colon. S100A4 was mainly localised in the colorectal tumour-associated stroma, it was also detectable in a limited number of epithelial tumour cells. PMID: 27750112 our results suggest the existence of evolutionarily conserved pathways used by S100A4 to promote metastatic dissemination PMID: 27927689 miR-187-3p inhibits the migration/metastasis and epithelial mesenchymal transition in hepatocellular carcinoma by targeting S100A4 expression. PMID: 27544906 our findings highlight nuclear S100A4 as a candidate therapeutic target in cholangiocarcinoma and establish a mechanistic rationale for the use of low-dose paclitaxel in blocking metastatic progression of cholangiocarcinoma PMID: 27328733 The increased content of collagen fibers and overexpression of S100A4 and P53 may play an important role in myocardial fibrosis of HCM, and they can be used in future HCM research. Blockade of S100A4 may have therapeutic potential in HCM by attenuating cardiac fibrosis. PMID: 26781584 The experimental and in silico results suggest two divergent evolutionary pathways: NMIIA and NMIIB evolved to possess S100A4-dependent and -independent regulations, respectively. PMID: 27029887 Results found that CNE-1 nasopharyngeal carcinoma cell (NPC) line expressing S100A4 showed significantly increased invasion ability in vitro and in vivo. Also, it seems that aberrant DNA hypomethylation of its promotor region might lead to the metastasis progression in EBV-associated NPC. PMID: 26292668 Oct-1 modifies S100A4 exchange between intra- and extracellular compartments in Namalwa cells and increases their sensitivity to glucocorticoids. PMID: 27096393 ChIP studies showed that the S100A4 protein binds to the GDF15 promoter, implicating S100A4 in GDF15 regulation at the transcriptional level. PMID: 27278086 Cell invasion (matrigel) was reduced only in the Hs578T cells (p < 0.01). Silencing decreased the expression of the prometastatic molecules S100A4 and TGFbetaR2 in both cell lines and CD44 in Hs578T cells .We conclude that ECM1 is a key player in the metastatic process and regulates the actin cytoskeletal architecture of aggressive breast cancer cells at least in part via alterations in S100A4 and Rho A. PMID: 27770373 Aberrant S100A4 expression may predictendometrial cancer (EC) progression and play an important role in regulating EC cell invasion through Epithelial-mesenchymal transition (EMT) regulation. PMID: 27109209 S100A4 could promote the invasion ability of breast cancer cells via EMT, more importantly, it could participate in EMT via regulating MMP2 in breast cancer. PMID: 26409452 our results demonstrate not only that high expression of S100A4 contributes to an aggressive phenotype of EC, but also that its elevated expression is closely related to the MELF histopathological pattern. PMID: 27348205 S100A4, A8, and A9 proteins represent promising marker genes to evaluate the risk potential of suspicious oral lesions in molecular pathology. PMID: 27294692 Increased S100A4 expression is associated with thyroid papillary carcinoma. PMID: 26715280 Comparative analysis of various tumor lines showed no clear correlation between the expression level of Mts1/S100A4 and the content of Oct-1. However, at stable transfection of tumor cells with Oct-1A, Oct-1L, and Oct-1X isoforms we detected an elevated level of Oct-1, which stimulated Mts1/S100A4 secretion. PMID: 27193714 We studied the expression of S100A4 and the total PHF10 protein in some human cancer cell lines. We have found that, in the cell lines studied, the PHF10 expression is correlated with the S100A4 expression. PMID: 27193724 These results support the hypothesis that S100A4 contributes significantly to growth and metastasis, and that down-regulation of S100A4 expression decreases the metastatic potential of ATC cells. PMID: 27802204 Interaction of extracellular S100A4 with RAGE prompts prometastatic activation of melanoma cells. PMID: 26928771 Study shows that negative expression of S100A4 was significantly associated with higher 3-year OS rate and N0 stage for lymph node metastasis in pancreatic neoplasm tumor which suggest that S100A4 expression represents a potential marker for lymph node metastasis and a potential unfavorable factor for prognosis of patients with this disease. PMID: 26903691 S100A4 mRNA level is an important molecular biomarker for prediction of chemosensitivity to gemcitabine in unresectable pancreatic cancer. PMID: 26722531 Tag7-Mts1 complex causes chemotactic migration of lymphocytes, with NK cells being a preferred target. PMID: 26654597 our data suggest a novel mechanism for mutant p53V143A accumulation and add a new facet to the role of S100A4 in cancer PMID: 26497012 S100A4 levels are elevated in human periodontal ligament cells in response to IL-1beta. PMID: 26499072 Enhanced S100A4 expression was observed in remodeled intrapulmonary arteries of COPD patients. PMID: 26483185 Downregulation of AKT3 increases migration and metastasis in triple negative breast cancer cells by upregulating S100A4. PMID: 26741489 vimentin and FSP1 have roles in gingival fibrosis PMID: 25826487 Through selective knockout or inhibition of the network components, we show that the interaction between epidermal growth factor receptor (EGFR) and S100A4 modulates the sensitivity of angiogenesis development to matrix metalloproteinases (MMPs) activity PMID: 26057862 The results show that S100A4 enhances the activity of matrix metalloproteinases (MMPs), causing higher cell dissociation. Moreover, it leads to an increased stability of the pathological state. PMID: 26118552 EZH2 mediates the regulation of E-cadherin expression by S100A4 and controls the proliferation and migration of gastric cancer cells. PMID: 26897964 Proximity ligation assay demonstrate proximity between S100A4 and cyclin B1 in vitro, while confocal microscopy showed S100A4 to localize to areas corresponding to centrosomes in mitotic cells prior to chromosome segregation. PMID: 26349943 Elevated S100A4 in plasma is a novel biomarker for early detection of acute myocardial infarction. PMID: 26166646 PTCSC3 downregulates S100A4, leading to a reduction in cell motility and invasiveness. We propose that PTCSC3 impacts papillary thyroid cancer predisposition and carcinogenesis through the S100A4 pathway. PMID: 26274343

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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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