| 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: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard phenotype marker for the identification of T cell populations. Mature human CD4 consists of a 371 amino acid (aa) extracellular region containing four immunoglobulin-like domains, a 22 aa transmembrane segment, and a 40 aa cytoplasmic domain. Within the ECD, human CD4 shares approximately 52% aa sequence identity with mouse and rat CD4. CD4 is expressed along with CD8 on double positive T cells during their development in the thymus. Either CD4 or CD8 expression is then lost, giving rise to single positive (SP) CD4+ or CD8+ mature T cells. CD4+ SP cells, also known as T helper cells, further differentiate into multiple subsets of CD4+ cells including Th1, Th2, Th17, Tfh, and Treg cells which regulate humoral and cellular immunity. CD4 is reexpressed on circulating CD8+ T cells upon activation and contributes to their cytotoxic effector activity. In human, CD4 is additionally expressed on macrophages, neutrophils, monocytes, NK cells, and neurons and glial cells in the brain. Similar CD4 distribution between species cannot be assumed as demonstrated by its presence on macrophages in human and rat but not in mouse. CD4 binds directly to MHC class II molecules on antigen presenting cells. This interaction contributes to the formation of the immunological synapse which is focused around the TCR-MHC class II-antigenic peptide interaction. Palmitoylation of two cysteine residues in the cytoplasmic tail of CD4 promotes the localization of CD4 in lipid rafts and its ability to augment TCR signaling via activation of the tyrosine kinase Lck. CD4 also functions as a chemotactic receptor for IL-16 and, in human, as a co-receptor for the gp120 surface glycoprotein of HIV-1... 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 |