![]() This will generate the template necessary to ensure it matches 100% when printing.ĥ. Put in your Avery Software/Re-Order Number. ![]() This will allow you to save designs and access them again later.Ĥ. Go to the Avery Design & Print website: ģ. Once you've finished editing, download the finished template in JPEG format (make sure to delete the outline prior to downloading, as you will not need it for pre-cut paper).Ģ. Please ask any questions prior to purchase.ġ. We can not guarantee that these will match any other kinds of pre-cut paper. You can print these on a home computer and cut them out by hand, upload them to a printing house or use AVERY pre-cut paper (**please refer to instructions below on how to print with Avery paper**). There is no expiry on the template, so you can come back and edit & save it as many times as you’d like. Edit, Download & Print as many times as you’d like! The email is sent instantly once your payment has been processed, but in some cases it can take 10-15 minutes.ģ. You will then be sent an email from Templett with a direct LINK to your purchased template/s. ![]() This is a digital item, nothing physical is shipped from us.Ģ. This is a template that you are required to edit yourself. Need a different size? Send us a message to discuss a size change order! Trim & Bleed line options are available, to assist with printing and cutting. Use Templett’s ‘Save Paper’ option to print multiple designs per page when downloading as a PDF. JPEG: Professional Printing & Digital distribution ![]() PDF: Ideal for Home & Professional Printing ➡ Square Gift Tag without an outline - 2x2 inches ➡ Round Gift Tag with an outline - 2x2 inches This purchase includes the following editable templates: You then have the option to print from home or at a print shop of your choosing. After purchase, you’ll receive an email from Templett which gives you a direct link to your purchase. Scale bars: 20 μm.You can edit this gift tag directly from your web browser on your computer using ! All fonts & graphics are pre-loaded for you, so you don’t need to download anything (other than your beautifully finished template!). Cells expressing mGPIHBP1-W108S did not bind cLPL-wt. ( B) Immunocytochemistry studies showing that cLPL-wt bound avidly to CHO cells expressing wild-type mGPIHBP1 (colocalization), while LPL-C420Y had no capacity to bind to cells expressing wild-type mGPIHBP1 (no colocalization). Cells expressing hGPIHBP1-W109S did not bind cLPL-wt. ![]() ( A) Immunocytochemistry studies showing that cLPL-wt bound avidly to neighboring CHO cells expressing wild-type hGPIHBP1 (hence cLPL-wt colocalized with hGPIHBP1), whereas cLPL-C420Y had no capacity to bind to cells expressing wild-type hGPIHBP1 (no colocalization). Immunocytochemistry studies were performed on permeabilized and nonpermeabilized cells with a goat antibody against the S-protein tag (red) and a mouse monoclonal antibody against the V5 tag (green). We conclude that LPL reaches the capillary lumen in chickens - as it does in mammals - despite an apparent absence of GPIHBP1.ĬHO pgsA-745 cells were transiently transfected with S-protein–tagged wild-type human (h) or mouse (m) GPIHBP1 (or hGPIHBP1-W109S or mGPIHBP1-W108S) and coplated with cells that had been transfected with V5-tagged versions of cLPL (wt or C420Y). However, we could not identify a gene for GPIHBP1 in the chicken genome, nor could we identify a transcript for GPIHBP1 in a large chicken RNA-seq data set. Remarkably, chicken LPL bound in a specific fashion to mammalian GPIHBP1. LPL was released rapidly from chicken hearts with an infusion of heparin, consistent with LPL being located inside blood vessels. When the antibodies against chicken LPL were injected intravenously into chickens, they bound to LPL on the luminal surface of capillaries in heart and adipose tissue. Using purified antibodies against chicken LPL, we showed that LPL is present on capillary endothelial cells of chicken heart and adipose tissue, colocalizing with von Willebrand factor. The obvious question is whether the LPL in lower vertebrates is able to reach the capillary lumen. In all lower vertebrate species (e.g., birds, amphibians, reptiles, fish), a gene for LPL can be found easily, but a gene for GPIHBP1 has never been found. In mammals, GPIHBP1 is absolutely essential for transporting lipoprotein lipase (LPL) to the lumen of capillaries, where it hydrolyzes the triglycerides in triglyceride-rich lipoproteins. ![]()
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