| Description | (Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) is a potent PTH-1R antagonist | 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>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds toPurity>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.Post-translationalA soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. O-glycosylated with core 1 or possibly core 8 glycans... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Interleukin 33 (IL-33), also known as DVS27 or NF-HEV (Nuclear Factor from High Endothelial Venules), is a pro-inflammatory protein and a chromatin-associated cytokine of the IL-1 family with high sequencePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Interleukin 33 (IL-33), also known as DVS27 or NF-HEV (Nuclear Factor from High Endothelial Venules), is a pro-inflammatory protein and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 protein is expressed highly and rather selectively by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyer's patches, and lymph nodes. IL-33 protein has transcriptional regulatory properties, and the researches suggested that IL-33 is a dual-function protein that might act both as a cytokine and as an intracellular nuclear factor. As a type 2 cytokines, IL-33 protein also play a pivotal role in helminthic infection and allergic disorders... Read More | As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a recombinant human serum albumin developed by using rice endosperm cell expression platform (oryzhiexp) and purification platform (oryzpur). It does not contain animal derived ingredients and can eliminate the risk of blood derived virus infection. Compared with fetal bovine serum (FBS), plasma derived albumin (pHSA) and bovine serum albumin (BSA), osrhsa has higher purity and better batch stability. It can be used in various research fields, including biopharmaceutical, cell therapy and cell culture of gene therapy. It can replace serum and promote cell growth. At the same time, osrhsa is also widely used in biomedical production as drug carrier, vaccine protector, cell cryoprotectant and medical device embedding agent.ApplicationBiopharmaceuticals, human vaccines, cell culture, cell storage, chemical drug molecular carriers, medical devices, in vitro diagnosis, etc.Comparison of physical and chemical properties between OsrHSA and natural human white pHSAphysicochemical propertiespHSAOsrHSAamino acid sequenceagreementN-terminal amino acidsDAHKSEVDAHKSEVC-terminal amino acidsKLVAASQAALGLKLVAASQAALGLGlycoside modificationnothingmolecular weight (MALDl)66.554 (kDa)66.550 ( a)Isoelectric point (pl)4.84.8Drug binding activityclosethermal stabilitymp 65℃mp 65℃esterase activityidenticalcrystal structureidenticalRestrictions on use:The above products are only suitable for scientific research, laboratory and production use, and cannot be directly used in human body... Read More |