Recombinant Mouse Protein S100-A8 (S100A8) Protein (His)

Name: Recombinant Mouse Protein S100-A8 (S100A8) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03354P
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 Mouse Protein S100-A8 (S100A8) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P27005
Target Symbol	S100A8
Synonyms	S100a8; Caga; Mrp8; Protein S100-A8; Calgranulin-A; Chemotactic cytokine CP-10; Leukocyte L1 complex light chain; Migration inhibitory factor-related protein 8; MRP-8; p8; Pro-inflammatory S100 cytokine; S100 calcium-binding protein A8
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	PSELEKALSNLIDVYHNYSNIQGNHHALYKNDFKKMVTTECPQFVQNINIENLFRELDINSDNAINFEEFLAMVIKVGVASHKDSHKE
Expression Range	2-89aa
Protein Length	Full Length of Mature Protein
Mol. Weight	12.2kDa
Research Area	Others
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	S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex is proposed to direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity.; (Microbial infection) Upon infection by murine coronavirus (MHV-A59), induces expansion of aberrant immature neutrophils in a TLR4-dependent manner.
Subcellular Location	Secreted. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation or endothelial adhesion of monocytes, is secreted via a microtubule-mediated, alternative pathway.
Protein Families	S-100 family
Database References	KEGG: mmu:20201 STRING: 10090.ENSMUSP00000064385 UniGene: PMID: 29263322 We present the reconstitution, purification, and characterization of mCP as well as the cysteine-null variant mCP-Ser. Apo mCP is a mS100A8/mS100A9 heterodimer, and Ca(II) binding causes two heterodimers to self-associate and form a heterotetramer PMID: 29659256 S100A8 was required for laser-induced new collagen synthesis in skin cells. PMID: 29270708 Chronic Pseudomonas aeruginosa biofilm infection reduces murine S100A8/ S100A9 expression and delays species-specific burn wound closure. PMID: 28645160 data suggest that S100A8/A9 acts directly on BV-2 microglial cells via binding to TLR4 and RAGE on the membrane and then stimulates the secretion of proinflammatory cytokines through ERK and JNK-mediated NF-kappaB activity in BV-2 microglial cells. PMID: 28498464 Like S100A8, S100A9 and S100A8/A9 reduced neutrophil influx in acute lung injury provoked by lipopolysaccharide (LPS) challenge. PMID: 28074060 theses findings reveal unexpected gene expression differences between WT and KO mice at a young age (in the absence of physiological stress), and address the hypothesis that Mrp8 and Mrp14 accumulation promotes age-related inflammation PMID: 27224926 S100A8 and S100A9 aggravate Coxsackievirus B3-induced myocarditis and might serve as therapeutic targets in inflammatory cardiomyopathies. PMID: 29158436 Neutrophil-derived S100A8/A9 promotes thrombocytosis in diabetic mice PMID: 28504650 Perinatal alarmins S100A8 and S100A9 specifically altered MyD88-dependent proinflammatory gene programs. S100 programming prevented hyperinflammatory responses without impairing pathogen defense. TRIF-adaptor-dependent regulatory genes remained unaffected by perinatal S100 programming and responded strongly to lipopolysaccharide, but were barely expressed. PMID: 28459433 S100a8 upregulation triggers NF-kappaB signal pathway through RAGE and TLR4, in response to laser-induced dermis wound healing. PMID: 26914682 Although MRP-8/-14 expression is highly increased in experimental, these proteins do not contribute to the pathogenesis in the effector phase of epidermolysis bullosa acquisita and bullous pemphigoid. PMID: 26692467 TLR4, TLR2 also contributed to Mrp8-induced inflammatory response and tolerance. PMID: 26329314 S100A8 appears to play a crucial role in the activation of the TLR4/MD-2 pathway and the promotion of a tumor growth-enhancing immune microenvironment. PMID: 26165843 S100A8 is primarily produced from CXCR2-expressing CD11b(+)Gr-1(high) cells, and it upregulates TNF-alpha production in CD11b(+)F4/80(+) cells through cellular cross-talk, which is an important mechanism in the development of Nonalcoholic fatty liver disease PMID: 26608915 Alarmins S100A8/S100A9 aggravate osteophyte formation in experimental osteoarthritis and predict osteophyte progression in early human symptomatic osteoarthritis. PMID: 25180294 Inflammation-induced S100A8 promotes colorectal tumorigenesis by acting upstream to activate the Akt1-Smad5-Id3 axis. PMID: 26135667 Data shows that S100A8/A9 plays a critical role during glomerulonephritis, exerting and amplifying autocrine and paracrine proinflammatory effects on bone marrow-derived macrophages, renal endothelial cells, and mesangial cells. PMID: 25759267 S100A8 could be a chemokine of oocyte origin, which attracts ovarian somatic cells to form the primordial follicles. PMID: 25953201 expression of S100A8 in the lungs may facilitate recruitment of MDSC, which may in turn aid in establishing a metastatic niche capable of suppressing a localized immune response. PMID: 25255046 This paper found a novel activation mechanism of NK cells via S100A8/A9-RAGE signaling, which may open a novel perspective on the in vivo interaction between inflammation and innate immunity. PMID: 25911757 data suggest that S100A8 exerts pro-inflammatory effect on the occurrence and development of neuro-inflammation and postoperative cognitive dysfunction by activating TLR4/MyD88 signaling in the early pathological process of the postoperative stage. PMID: 25449673 S100A8 and S100A9 initiate the early inflammatory program in injured peripheral nerves PMID: 25792748 Time-lapse intravital multiphoton imaging of adipose tissues identified the very early event exhibiting increased mobility of macrophages, which may be triggered by increased expression of adipose S100A8. PMID: 25848057 Myocardial gene and protein expression of S100A8 was also significantly increased in mice 1 day after debanding that had been preceded by 3 days or 1 week of transverse aortic constriction. PMID: 25820336 THC-induced myeloid-derived suppressor cells secreted elevated levels of S100A8. Neutralization of S100A8 in vivo reduced the ability of THC to trigger MDSCs. High S100A8 expression also promoted their suppressive function. PMID: 25713087 Calprotectin heterodimer of subunits S100A8 (and S100A9 ) is detectable within 6 h of infection as immune cells respond to the invading pathogen. PMID: 23754577 Myeloid-related proteins 8 and 14 contribute to monosodium urate monohydrate crystal-induced inflammation in gout. PMID: 24470119 S100A8/A9 expression in the skin epidermal layer has a role in controlling skin tumor formation PMID: 24436096 Data indicate that angiotensin II infusioni increased expression of S100a8/a9 in the heart. PMID: 24711518 S100a8 and S100a9, associated with immune responses, were common differentially expressed genes in a mouse model of hereditary hemochromatosis. PMID: 24338419 These results suggest that S100A8 alarmin is sufficient, but not necessary, to induce polymorphonuclear neutrophil migration during vulvovaginal candidiasis and this responseinvolves pattern recognition receptors. PMID: 24478092 depletion increased Pseudomonas aeruginosa burden in flagellin-pretreated corneas PMID: 23340821 These results suggest that rapid secretion of MRPs by neutrophils at the site of infection may protect uninfected macrophages and favor a more efficient innate inflammatory response against Leishmania infection. PMID: 24086787 High levels of S100A8/A9 proteins aggravate ventilator-induced lung injury via TLR4 signaling. PMID: 23874727 S100A8 and ephrin-A1 contribute to lung metastasis. PMID: 24103748 Our study demonstrated a dual role for MRP8/14 in bacterial keratitis. PMID: 23299480 results identify MRP8/14 as key player in protective innate immunity during Klebsiella pneumonia PMID: 23133376 Mrp8, the active component of the heterocomplex, inhibits early dendritic cells (DCs) maturation and antigen presentation in a TLR-4-dependent manner. PMID: 23188082 S100A8 and S100A9 proteins are crucially involved in synovial activation and cartilage destruction during osteoarthritis. PMID: 22143922 S100A8 and S100A9 were specifically induced by LPS in the salivary glands. PMID: 21125321 sustained activation of S100A8/A9 critically contributes to the development of post-ischemic heart failure (HF) driving the progressive course of HF through activation of RAGE. PMID: 22318783 Targeted imaging with myeloid-related protein 8/14 via gadolinium immunonanoparticles demonstrates enhancement of plaque with binding to inflammatory cells and reduction in inflammation. PMID: 22308043 S100a8, without S100a9, has a previously unrecognized role in embryo development. S100a8 also has a second role in the maternal deciduum, where expression is associated with the vasculature from the E8.5 stage to the formation of mature placenta. PMID: 22016186 The calcium-binding proteins myeloid-related protein (MRP)-8 (S100A8) and MRP-14 (S100A9) form MRP-8/14 heterodimers (S100A8/A9, calprotectin) that regulate myeloid cell function and inflammatory responses in graft rejectionl PMID: 22144572 Rab30 and S100a8/S100a9 were indicated to play roles in the initiation of liver regeneration as well as possibly in the functional switch of the liver in the newborn stage. PMID: 21308349 These results thus reveal a novel role for myeloid-derived S100A8/A9 in activating specific downstream genes associated with tumorigenesis and in promoting tumor growth and metastasis. PMID: 21228116 These results demonstrate that S100A8 stimulated osteoclast formation and activity and suggest that both S100A8 and TLR-4 are important factors in mediating osteoclastic bone destruction in experimental arthritis. PMID: 21337316 The results may provide important information for the expression of s100a8/a9 and RAGE, linking progressive cystogenesis with inflammation in cystic kidney. PMID: 20606421 Chondrocyte derived S100A8 and S100A9 may have a sustained role in cartilage degradation in inflammatory arthritis PMID: 20105291

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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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