Calprotectin (S100a8) (NM_013650) Mouse Recombinant Protein

CAT#: TP721199L

Purified recombinant protein of Mouse S100 calcium binding protein A8 (calgranulin A) (S100a8)

Specifications

Product Data

• Species: Mouse
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  Met1-Glu89
• Tag: C-His
• Predicted MW: 11.3 kDa
• Concentration: lot specific
• Purity: >95% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: Provided lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl
• Endotoxin: Endotoxin level is < 0.1 ng/µg of protein (< 1 EU/µg)
• Reconstitution: Always centrifuge tubes before opening. Do not mix by vortex or pipetting. Dissolve the lyophilized protein in ddH2O. It is not recommended to reconstitute a concentration less than 100 µg/ml. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
• Storage: Store at -80°C.
• Stability: Stable for at least 6 months from date of receipt under proper storage and handling conditions.

Reference Data

• RefSeq: NP_038678
• Locus ID: 20201
• UniProt ID: P27005, Q53X15
• Cytogenetics: 3 39.9 cM
• Refseq Size: 392
• Refseq ORF: 267
• Synonyms: 60B8Ag; AI323541; B8Ag; Caga; CFAg; CP-10; MRP8; p8
• Summary: 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 (By similarity).[UniProtKB/Swiss-Prot Function]