Recombinant Mouse MRP8 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9965P

Recombinant Mouse MRP8 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9965P
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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 (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 26 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

Gene Functions References

  1. Specific NLRC4 activation in Mrp8 (+) cells (primarily neutrophil lineage) is sufficient to cause severe inflammatory disease. PMID: 29263322
  2. 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
  3. S100A8 was required for laser-induced new collagen synthesis in skin cells. PMID: 29270708
  4. Chronic Pseudomonas aeruginosa biofilm infection reduces murine S100A8/ S100A9 expression and delays species-specific burn wound closure. PMID: 28645160
  5. 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
  6. Like S100A8, S100A9 and S100A8/A9 reduced neutrophil influx in acute lung injury provoked by lipopolysaccharide (LPS) challenge. PMID: 28074060
  7. 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
  8. S100A8 and S100A9 aggravate Coxsackievirus B3-induced myocarditis and might serve as therapeutic targets in inflammatory cardiomyopathies. PMID: 29158436
  9. Neutrophil-derived S100A8/A9 promotes thrombocytosis in diabetic mice PMID: 28504650
  10. 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
  11. S100a8 upregulation triggers NF-kappaB signal pathway through RAGE and TLR4, in response to laser-induced dermis wound healing. PMID: 26914682
  12. 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
  13. TLR4, TLR2 also contributed to Mrp8-induced inflammatory response and tolerance. PMID: 26329314
  14. 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
  15. 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
  16. Alarmins S100A8/S100A9 aggravate osteophyte formation in experimental osteoarthritis and predict osteophyte progression in early human symptomatic osteoarthritis. PMID: 25180294
  17. Inflammation-induced S100A8 promotes colorectal tumorigenesis by acting upstream to activate the Akt1-Smad5-Id3 axis. PMID: 26135667
  18. 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
  19. S100A8 could be a chemokine of oocyte origin, which attracts ovarian somatic cells to form the primordial follicles. PMID: 25953201
  20. 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
  21. 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
  22. 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
  23. S100A8 and S100A9 initiate the early inflammatory program in injured peripheral nerves PMID: 25792748
  24. 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
  25. 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
  26. 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
  27. Calprotectin heterodimer of subunits S100A8 (and S100A9 ) is detectable within 6 h of infection as immune cells respond to the invading pathogen. PMID: 23754577
  28. Myeloid-related proteins 8 and 14 contribute to monosodium urate monohydrate crystal-induced inflammation in gout. PMID: 24470119
  29. S100A8/A9 expression in the skin epidermal layer has a role in controlling skin tumor formation PMID: 24436096
  30. Data indicate that angiotensin II infusioni increased expression of S100a8/a9 in the heart. PMID: 24711518
  31. S100a8 and S100a9, associated with immune responses, were common differentially expressed genes in a mouse model of hereditary hemochromatosis. PMID: 24338419
  32. 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
  33. depletion increased Pseudomonas aeruginosa burden in flagellin-pretreated corneas PMID: 23340821
  34. 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
  35. High levels of S100A8/A9 proteins aggravate ventilator-induced lung injury via TLR4 signaling. PMID: 23874727
  36. S100A8 and ephrin-A1 contribute to lung metastasis. PMID: 24103748
  37. Our study demonstrated a dual role for MRP8/14 in bacterial keratitis. PMID: 23299480
  38. results identify MRP8/14 as key player in protective innate immunity during Klebsiella pneumonia PMID: 23133376
  39. Mrp8, the active component of the heterocomplex, inhibits early dendritic cells (DCs) maturation and antigen presentation in a TLR-4-dependent manner. PMID: 23188082
  40. S100A8 and S100A9 proteins are crucially involved in synovial activation and cartilage destruction during osteoarthritis. PMID: 22143922
  41. S100A8 and S100A9 were specifically induced by LPS in the salivary glands. PMID: 21125321
  42. 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
  43. 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
  44. 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
  45. 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
  46. 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
  47. 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
  48. 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
  49. The results may provide important information for the expression of s100a8/a9 and RAGE, linking progressive cystogenesis with inflammation in cystic kidney. PMID: 20606421
  50. 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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