Recombinant Mouse MRP8 Protein (His tag)

Name: Recombinant Mouse MRP8 Protein (His tag)
Brand: Beta LifeScience
SKU: BLA-9964P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Mouse
Accession	P27005
Synonym	60B8Ag AI323541 B8Ag BEE11 CAGA Calgranulin-A Calprotectin L1L subunit Calprotectin, included CFAG CGLA Chemotactic cytokine CP-10 CP-10 Cystic fibrosis antigen L1Ag Leukocyte L1 complex light chain MA387 MIF Migration inhibitory factor-related protein 8 MRP-8 Myeloid-related protein 8 Neutrophil cytosolic 7 kDa protein NIF p8 Pro-inflammatory S100 cytokine Protein S100-A8 S100 calcium binding protein A8 S100 calcium binding protein A8 (calgranulin A) S100 calcium-binding protein A8 S100A8 S100A8/S100A9 complex, included S10A8_HUMAN Urinary stone protein band A
Description	Recombinant Mouse MRP8 Protein (His tag) was expressed in Yeast. It is a Full length protein
Source	Yeast
AA Sequence	PSELEKALSNLIDVYHNYSNIQGNHHALYKNDFKKMVTTECPQFVQNINI ENLFRELDINSDNAINFEEFLAMVIKVGVASHKDSHKE
Molecular Weight	12 kDa including tags
Purity	>90% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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: Mm.21567

Gene Functions References

Specific NLRC4 activation in Mrp8 (+) cells (primarily neutrophil lineage) is sufficient to cause severe inflammatory disease. 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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