Recombinant Human Protein S100-A1 (S100A1) Protein (His-SUMO)

Name: Recombinant Human Protein S100-A1 (S100A1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09941P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein S100-A1 (S100A1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P23297
Target Symbol	S100A1
Synonyms	Bpb; NEF; Protein S100-A1; S-100 protein alpha chain; S-100 protein subunit alpha; S100 alpha; S100 beta; S100 calcium binding protein A1; S100 calcium binding protein B; S100 calcium-binding protein A1; S100 protein alpha polypeptide; S100A; s100a1; S100B; S100beta; S10A1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
Expression Range	2-94aa
Protein Length	Partial
Mol. Weight	26.4kDa
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.
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	Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. These changes allow interactions with specific target proteins and modulate their activity. Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase. Facilitates diastolic Ca(2+) dissociation and myofilament mechanics in order to improve relaxation during diastole.
Subcellular Location	Cytoplasm. Sarcoplasmic reticulum. Mitochondrion.
Protein Families	S-100 family
Database References	HGNC: 10486 OMIM: 176940 KEGG: hsa:6271 STRING: 9606.ENSP00000292169 UniGene: PMID: 29240297 Data found that S100A1 was upregulated in hepatocellular carcinoma (HCC) tissues, and its upregulation was associated with large tumor size, low differentiation, and shorter survival rates. Further results supports the hypothesis that S100A1 functions as an oncogene and may be a biomarker for the prognosis of patients with HCC. S100A1 exerted its oncogenic function by interacting with LATS1 and activating Hippo pathway. PMID: 29901195 The results indicate that changes in the circulating level of S100A1 protein occur in metabolic syndrome patients. The strong correlation between serum zinc-alpha2-glycoprotein and S100A1 might suggest that production or release of these two proteins could be related mechanistically. PMID: 28825380 The results indicated that S100A1 enhanced the ovarian cancer cell proliferation and migration. PMID: 28595036 found that S100B plays a crucial role in blocking the interaction site between RAGE V domain and S100A1. A cell proliferation assay WST-1 also supported our results. This report could potentially be useful for new protein development for cancer treatment PMID: 29444082 Study provides evidence that mir-363 and its target S100A1 are under the regulatory function of FOXD2-AS1 aggravating nasopharyngeal carcinoma carcinogenesis. PMID: 29248577 X-ray crystal structure of human calcium-bound S100A1 has been reported. PMID: 28368280 a molecular mechanism for the potential regulation of TRPM1 by S100A1 PMID: 27435061 Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 are key players in this pathway; the stoichiometry of S100A1/STIP1 interaction appears to be three S100A1 dimers plus one STIP1 monomer; each S100A1-STIP1-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 = stress-induced-phosphoprotein 1) [REVIEW] PMID: 28819010 Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1. PMID: 28408431 Results identified amino acids motif in S100A1 for protein binding to 2-oxohistidine which appears to be an evolutionarily conserved capacity from bacteria to human. PMID: 27644758 a correlation between S100B + A1-positive Human Articular Chondrocytes in monolayer culture and their neochondrogenesis capacity in pellet culture, is reported. PMID: 27861869 In line with these observations, rhesus monkey rhadinovirus infection resulted in rapid degradation of SP100, followed by degradation of PML and the loss of ND10 structures, whereas the protein levels of ATRX and DAXX remained constant. PMID: 27356898 High Serum protein S100 levels are associated with postoperative delirium after off-pump coronary artery bypass surgery. PMID: 26943607 molecular dynamics simulations of S100A1 in the apo/holo (Ca(2+)-free/bound) states, is reported. PMID: 26958883 The relationship between the degree of infiltration by S100-positive (S100+) dendritic cells and prognostic factors, including histological subtype, histological grade, peritumor inflammatory infiltration, and stromal desmoplasia, were examined. PMID: 25611268 In this review, we aim to describe the molecular basis and regulatory function of S100A1--{REVIEW} PMID: 25157660 Patients with acute myocardial infarction (MI) showed significantly increased S100A1 serum levels. S100A1 signaling in cardiac fibroblasts occurs through endosomal TLR4/MyD88. PMID: 24833748 hypoxia-induced MiR-138 is an essential mediator of EC dysfunction via its ability to target the 3'UTR of S100A1. PMID: 24244340 It was suggested that S100A1 and S100B be used as markers to develop potency assays for cartilage regeneration cell therapies, and as a redifferentiation readout in monolayer cultures aiming to investigate stimuli for chondrogenic induction. PMID: 24402969 Twenty-seven out of thirty-two (84.38%) cases of serous ovarian carcinoma were found to express S100A1. S100A1 expression was observed in one out of the two mucinous and three out of the six endometroid ovarian carcinomas. PMID: 24501865 The triple mutation Arg852/Lys859/Arg860 exhibited significant disruption of the binding of S100A1 to TRPC6 implicating their involvement in the binding site. PMID: 23671622 For autopsy material, all human cases of definite myocardial infarction and suspected early infarction showed well-defined areas without S100A1 staining. PMID: 23683996 This study showed that overexpression of S100A10, may play a role in irritable bowel syndrome, and that the IL10-819 CC is a candidate genotype for irritable bowel syndrome and ulcerative colitis. PMID: 23595519 In this review we will focus on the roles of S100A proteins in intracellular and extracellular calcium signalling and homeostasis. PMID: 23662436 the increased calcium binding affinity of S100A1 upon thionylation arises, most probably, from rearrangement of the hydrophobic core in its apo form PMID: 23351007 Report downregulation of S100A1 expression in critical limb ischemia impairs postischemic angiogenesis via compromised proangiogenic endothelial cell function and nitric oxide synthase regulation. PMID: 23048072 S-Nitrosylation of S100A1 increases Ca(2+) binding and tunes the overall protein conformation. PMID: 22989881 Uremia clearance using NHD is accompanied by improvement in LV strain, rotation, reduction in mass and volume index. Dialysis downregulates genes for cardiomyocyte apoptosis and fibrosis and upregulates S100A1, which may improve LV contractility. PMID: 22647434 Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel. PMID: 22451665 The three-dimensional structure of human apo(calcium free)S100A1 protein was determined by NMR spectroscopy PMID: 21296671 Thermodynamics of zinc binding to human S100A2 PMID: 21090249 S100A1, S100A2, S100A4, S100A6 and S100B interacted with MDM2 (2-125). PMID: 20591429 A single phenyl-Sepharose column was sufficient for the purification of human S100A11 whereas HiTrap Q anion exchange followed by phenyl-Sepharose columns were required for the purification of S100A1. PMID: 20347987 The expression of S100A1 was low in benign melanocytic tumours and increased in malignant melanomas PMID: 20042890 S100A1B and S100BB are increased in urine collected from asphyxiated newborns who will develop hypoxic-ischemic encephalopathy (HIE) since first urination, and their measurement may be useful to early predict HIE. PMID: 19482672 S100A1 is a specific and sensitive immunohistochemical marker to differentiate nephrogenic adenoma from prostatic adenocarcinoma PMID: 19384190 The presence of the S100A1 in myocardial sarcoplasmic reticulum and myofibrils may be related to the known target proteins for S100A1 at these sites. PMID: 11829317 Impaired cardiac contractility response to hemodynamic stress in S100A1-deficient mice. PMID: 11909974 identification of the S100A1 C terminus (amino acids 75-94) and hinge region (amino acids 42-54) to differentially enhance sarcoplasmic reticulum Ca2+ release with a nearly 3-fold higher activity of the C terminus PMID: 12721284 S100A1 has a reglatory role in the contraction-relaxation cycle in the human heart PMID: 12804600 S100A1 protein serves as a cardioprotective factor in vitro PMID: 12960148 identified S100A1, but not calmodulin or other S100 proteins, as a potent molecular chaperone and a new member of the Hsp70/Hsp90 multichaperone complex PMID: 14638689 Synapsins and S100A1 interact in nerve terminals where coexpresssed; S100A1 cannot bind SV-associated synapsin I and may function as a cytoplasmic store of monomeric synapsin I; synapsin dimerization and interaction with S100A1 are mutually exclusive PMID: 15147519 Results demonstrate that restoration of S100A1 protein levels in failing myocardium by gene transfer may be a novel therapeutic strategy for the treatment of heart failure. PMID: 15578088 This study provides the first evidence that intracellular S100A1, depending on its subcellular location, modulates cardiac Ca2+-turnover via different Ca2+-regulatory proteins. PMID: 15654019 S100A1 was expressed in 2/15 clear cell RCCs, 11/15 papillary RCCs, 7/8 oncocytomas and in 0/7 chromophobe RCCs. PMID: 15780567 the three-dimensional structure of calcium-bound S100A1 was determined by multidimensional NMR spectroscopy and compared to the previously determined structure of apo-S100A1 PMID: 16169012 S-100 protein expression in tumour cells was associated with significantly decreased survival PMID: 16760135 analysis of the different reactivity pattern of S100A1 in the external auditory canal cholesteatoma PMID: 16969478

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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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