| Description | If the serum will not be used up within a short period of time, dispense after thawing and store aliquot under appropriate conditions for long-term storage. The volume of serum will increase by 10% after freezing, so when dispensing serum into tubes, leave some space in the tube to avoid tube If the serum will not be used up within a short period of time, dispense after thawing and store aliquot under appropriate conditions for long-term storage. The volume of serum will increase by 10% after freezing, so when dispensing serum into tubes, leave some space in the tube to avoid tube cracking during the freezing.After the serum is thawed completely, the serum can be heated at 56℃ for 30 minutes to inactivate the complement in serum. Unless necessary, heat-inactivation of the serum is not recommended for general use because heat treatment will result in precipitation of serum and decreasing of serum quality. Complement is involved in reactions such as cytotoxicity, contraction of smooth muscle cells, release of histamine from mast cells and platelets, enhancement of phagocytosis, and promotion of chemical chemotaxis and activation of lymphocytes and macrophages.The serum should be thawed slowly and gradually. Thaw the serum stored at -15~-40℃ in 4℃ refrigerator for approximately one day, and make aliquot after it is thawed thoroughly. During the thawing process, shake gently every 2 hours (avoid the formation of air bubbles) to homogenize the component and reduce the occurrence of precipitation. Do not thaw the serum stored at -20℃ or lower temperatures directly in a 37℃ water bath to avoid protein agglomeration and precipitation in serum due to large temperature changes.The floc-like precipitates in serum are mainly denatured fibrin and lipoproteins in serum after long-term storage at 4℃. These flocs do not affect the quality of the serum and can be left untreated. If necessary, the flocs can be removed by centrifugation at 400×g for 5 minutes. However, it is not advisable to remove by filtration as the flocs may block the filter membrane. The precipitates in the serum after heat inactivation will increase significantly. Some of these deposits look like "black dots" under the microscope and are often misinterpreted as microbial contamination because the Brownian motion of these "dots" is magnified under the microscope and appear to be swimming. Usually, these small black spots do not affect cell growth, but if microbial contamination of the serum is suspected, it should be immediately replaced with new serum. Users can dilute the serum with culture medium to 10% concentration and incubate for 1-3 days, and observe whether the small black dots increase sharply, or spread an appropriate amount of serum on LB plate to determine whether there is microbial contamination. Do not leave the serum at 37℃ for too long, as the serum will gradually become cloudy and lose some active ingredients, thus affecting the quality of the serum.This product is for R&D only. Not for drug, household, or other uses.For your safety and health, please wear a lab coat and disposable gloves during the operation... Read More | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map (PubMed:23307924). Required for normal formation of bones and joints in the limbs, skull, digits and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal strucutres. Seems to positively regulates differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG (PubMed:26643732). Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Interleukin-6 (IL-6) is a pleiotropic, alpha-helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism,Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Interleukin-6 (IL-6) is a pleiotropic, alpha-helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression. Mature human IL-6 is 183 amino acids (aa) in length and shares 39% aa sequence identity with mouse and rat IL-6. Alternative splicing generates several isoforms with internal deletions, some of which exhibit antagonistic properties. IL-6 induces signaling through a cell surface heterodimeric receptor complex composed of a ligand-binding subunit (IL-6 R alpha) and a signal-transducing subunit (gp130). IL-6 binds to IL-6 R alpha, triggering IL-6 R alpha association with gp130 and gp130 dimerization. Gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM. Soluble forms of IL-6 R alpha are generated by both alternative splicing and proteolytic cleavage. In a mechanism known as trans-signaling, complexes of soluble IL-6 and IL-6 R alpha elicit responses from gp130-expressing cells that lack cell surface IL-6 R alpha. Trans-signaling enables a wider range of cell types to respond to IL-6, as the expression of gp130 is ubiquitous, while that of IL-6 R alpha is predominantly restricted to hepatocytes, monocytes, and resting lymphocytes. Soluble splice forms of gp130 block trans-signaling from IL-6/IL-6 R alpha but not from other cytokines that use gp130 as a co-receptor. IL-6, along with TNF-alpha and IL-1, drives the acute inflammatory response and the transition from acute inflammation to either acquired immunity or chronic inflammatory disease. When dysregulated, it contributes to chronic inflammation in obesity, insulin resistance, inflammatory bowel disease, arthritis, sepsis, and atherosclerosis. IL-6 can also function as an anti-inflammatory molecule, as in skeletal muscle where it is secreted in response to exercise. In addition, it enhances hematopoietic stem cell proliferation and the differentiation of Th17 cells, memory B cells, and plasma cells... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic orPurity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic or heterophilic cell-cell interactions. NCAM-1 specifically binds to heparan sulfate proteoglycans, the extracellular matrix protein agrin, and several chondroitin sulfate proteoglycans that include neurocan and phosphocan. There are three main forms of human NCAM-1 that arise by alternate splicing. These are designated NCAM-120/NCAM-1 (761 amino acids [aa]), NCAM‑140 (848 aa), and NCAM-180 (1120 aa). NCAM-120 is GPI-linked, while NCAM‑140 and NCAM-180 are type I transmembrane glycoproteins. Additional alternate splicing adds considerable diversity to all three forms, and extracellular proteolytic processing is possible for NCAM-180. NCAM-1 is synthesized as a 761 aa preproprecursor that contains a 19 aa signal sequence, a 722 aa GPI-linked mature region, and a 20 aa C-terminal prosegment. The molecule contains five C-2 type Ig-like domains and two fibronectin type-III domains. Human to mouse, NCAM-1 is 93% aa identical. NCAM-1 appears to be highly sialylated. The polysialyation of NCAM-1 reduces its adhesive property and increases its neurite outgrowth promoting features. NCAM-1 in the adult brain shows a decline of sialylation relative to earlier developmental periods. In regions that retain a high degree of neuronal plasticity, however, the adult brain continues to express polysialylation-NCAM-1, suggesting sialylation of NCAM-1 is involved in regenerative processes and synaptic plasticity... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity.Post-translationalN-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) are produced by proteolytic cleavage after secretion from peripheral blood monocytes... Read More |