| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | Inquire | 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%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in the ER. When secreted, it mediates chemotaxis and T cell adhesion to fibronectin. This is likely due to its prolyl cis/trans isomerase activity. Intracellularly, Cyclophilin B appears to serve as a molecular chaperone for molecules destined for secretion. It does so via stabilization and facilitating the activity of additional chaperones. The human CyPB precursor is 216 amino acids (aa) in length. It contains a 25 aa signal sequence plus a 191 aa mature region. There is a partial heparin-binding sequence (aa 27‑34), a PPIase domain (aa 47‑204), and a C-terminal ER retention motif (aa 213‑216). Over aa 34‑216, the human and mouse sequences are 95% aa identical... Read More | Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer... Read More |