| Description | LTBR Human Pre-designed siRNA Set A contains three designed siRNAs for LTBR gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components LTBR siRNA-1: 5 nmol (HPLC) LTBR siRNA-2: 5 nmol (HPLC) LTBR siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 LTBR Human Pre-designed siRNA Set A contains three designed siRNAs for LTBR gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components LTBR siRNA-1: 5 nmol (HPLC) LTBR siRNA-2: 5 nmol (HPLC) LTBR siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Human B7 homolog 3 (B7-H3) is a member of the B7 family of immune proteins that provide signals for the regulation of immune responses. Other family members include B7-1, B7-2, B7-H1/PD-L1, B7-H2, and PD-L2. B7 family proteins are type I transmembrane immunoglobulin (Ig) superfamily members that contain extracellular Ig V‑like and Ig C‑like domains with a short cytoplasmic tail. Among the family members there is about 20 - 40% amino acid (aa) sequence identity. B7-H3 was initially reported to be a 316 aa type I transmembrane precursor protein that contained a signal sequence, an extracellular region with one V‑type and one C‑type Ig domain, a transmembrane segment and a short cytoplasmic tail. Subsequent studies have identified a second 110 kDa form whose precursor is 534 aa in length. Termed 4IgB7-H3 or B7-H3b, this molecule has two additional Ig-like domains (one V‑type and one C‑type) and shows a ubiquituous expression pattern. It would appear that the human 4Ig form is the principal, if not the only form of B7-H3. Its precursor contains a 26 aa signal sequence, a 435 aa extracellular region, a 31 aa transmembrane domain, and a 42 aa cytoplasmic tail. The four Ig-like domains alternate between V‑type and C‑type, and apparently are the consequence of a V‑C type tandem duplication. B7-H3b is expressed on dendritic cells as well as activated T, B and NK cells. The mouse gene differs from that of human in that it cannot code for four Ig-like domains; only a V‑type:C‑type pair. Human B7-H3b binding to an undefined receptor has shown to be inhibitory to NK cell illing and cytokine release. It also seems to be required for late stage osteoblast differentiation... Read More | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More | Purity≥95% SDS-PAGE. Recombinant human MIF, fused to His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.FunctionPro-inflammatory cytokine. Involved in the innate immune response to Purity≥95% SDS-PAGE. Recombinant human MIF, fused to His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.FunctionPro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |