| Description | Reconstitute with 1.0 M acetic acid to the pre-lyophilization volume. Dilutions must be made in Acetic Acid.IgM heavy chain (mu chain) consists of 576 amino acids; there are five mu chains in each IgM molecule. IgM heavy chain is purified by reducing the disulfide bond connecting it to the IgM kappaReconstitute with 1.0 M acetic acid to the pre-lyophilization volume. Dilutions must be made in Acetic Acid.IgM heavy chain (mu chain) consists of 576 amino acids; there are five mu chains in each IgM molecule. IgM heavy chain is purified by reducing the disulfide bond connecting it to the IgM kappa and lambda light chains. IgM mu chain is more highly conserved across different species than is the heavy chain of IgG or IgA.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.Ref:Hayzer, D. J., and Jaton, J-C. 1985. Methods Enzymol. 116, 16; Jeske, D. J., and Capra J. D. 1984. Fundamental Immunology (W.E. Paul, ed.), 131... Read More | Inquire | Inquire | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein,Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein, released actively following cytokine stimulation as well as passively during cell death. It is the prototypic damage-associated molecular pattern (DAMP) molecule and has been implicated in several inflammatory disorders. HMGB1 signals via the receptor for advanced glycation end-product (RAGE) and members of the toll-like receptor (TLR) family. The most prominent HMGB1 protein and mRNA expression arthritis are present in pannus regions, where synovial tissue invades articular cartilage and bone. HMGB1 promotes the activity of proteolytic enzymes, and osteoclasts need HMGB1 for functional maturation. As a non-histone nuclear protein, HMGB1 has a dual function. Inside the cell, HMGB1 binds DNA, regulating transcription, and determining chromosomal architecture. Outside the cell, HMGB1 can serve as an alarmin to activate the innate system and mediate a wide range of physiological and pathological responses. Extracellular HMGB1 represents an optimal " necrotic marker" selected by the innate immune system to recognize tissue damage and initiate reparative responses. However, extracellular HMGB1 also acts as a potent pro-inflammatory cytokine that contributes to the pathogenesis of diverse inflammatory and infectious disorders. HMGB1 has been successfully therapeutically targeted in multiple preclinical models of infectious and sterile diseases including arthritis. As shown in studies on patients as well as animal models, HMGB1 can play an important role in the pathogenesis of the rheumatic disease, including rheumatoid arthritis, systemic lupus erythematosus, and polymyositis among others. Besides, enhanced postmyocardial infarction remodeling in type 1 diabetes mellitus was partially mediated by HMGB1 activation... Read More | Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal hematopoietic function and plays an important role in hematopoiesis, spermatogenesis, and melanogenesis. It also promotes mast cell adhesion, migration, proliferation, and survival. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant murine SCF is an 18.4kDa polypeptide containing 165 amino acid residues.Purity＞97% (SDS-PAGE,HPLC)FunctionLigand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.Post-translationalA soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain. Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. A soluble form exists as a cleavage product of the extracellular domain... Read More |