| Description | The HeLa protein digestion standard is a protein sample derived from HeLa cells and subjected to enzymatic hydrolysis, which is used for mass spectrometry analysis. Its main functions include quality control, method development, quantitative analysis, protein identification, and modification The HeLa protein digestion standard is a protein sample derived from HeLa cells and subjected to enzymatic hydrolysis, which is used for mass spectrometry analysis. Its main functions include quality control, method development, quantitative analysis, protein identification, and modification analysis. It is an indispensable tool in mass spectrometry analysis, capable of improving the accuracy and reliability of the analysis.Storage and Transportation:Storage: The lyophilized powder is stable for 2 years when stored at -20°C or below. The reconstituted and aliquoted product can be stored at -80°C for 1 year. Avoid repeated freezing and thawing!Transportation: It is recommended to transport with ice packs to maintain low temperature.Operating Procedures: 1.Preparation: It is recommended to dissolve the product with 0.1% FA (formic acid) solution. For example: take 1 tube of 20µg HeLa protein digestion standard lyophilized powder, add 40µL of 0.1% FA (formic acid) solution to dissolve it, and vortex to dissolve. The final concentration is 0.5µg/µL, and aliquot for storage.2.Loading: Use an appropriate amount for loading. Generally, 500ng is recommended for a 60-minute gradient, and 1-2µg for a 120-minute gradient. Inject the peptide standard solution into the mass spectrometer for analysis.Precautions and Disclaimer:1.This product is limited to scientific research use by professionals, and shall not be used for clinical diagnosis or treatment, nor for food or drugs.2.For your safety and health, please wear a lab coat and disposable gloves and masks during operation... Read More | Inquire | Inquire | Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen Purity>97% SDS-PAGE and HPLC analyses. FunctionLA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.Post-translationalProteolytic removal of residues 1-9 produces the active peptide connective tissue-activating peptide III (CTAP-III) (low-affinity platelet factor IV (LA-PF4)). Proteolytic removal of residues 1-13 produces the active peptide beta-thromboglobulin, which is released from platelets along with platelet factor 4 and platelet-derived growth factor. NAP-2(1-66) is produced by proteolytical processing, probably after secretion by leukocytes other than neutrophils. NAP-2(73) and NAP-2(74) seem not be produced by proteolytical processing of secreted precursors but are released in an active form from platelets... Read More | Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Currently, the Fn is purified from the plasma, which however is limited by the availability of supply. The the recombinant human fibronectin (OsrhFN) was expressed in the rice endosperm platform, which is animal component free and has high purity, and has been demonstrated has the same physical and chemical with the plasma derived Fn. OsrhFN provides a safety solution to replace the plasma derived FN.pH value: 6.0-8.0... Read More |