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The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegans and laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3).
The basic process by which imaging particle analysis is carried out is as follows: A digital camera captures an image of the field of view in the optical system.; A gray scale thresholding process is used to perform image segmentation, segregating out the particles from the background, creating a binary image of each particle.
Confocal microscopic analysis of a dermal fibroblast in primary culture from a control (a and b) and the subject with HGPS (c and d). Labelling was performed with anti-lamin A/C antibodies. Note the presence of irregularly shaped nuclear envelopes in many of the subject's fibroblasts
Particle size analyzers are used also in biology to measure protein aggregation. Particle size distribution of antiviral vaccines subjected to cold-chain disruptions, analyzed by Dynamic Light Scattering (DLS) DLS is a particularly appreciated technique for the characterization of nanoparticles designed for drug delivery, such as vaccines.
Single particle analysis is a group of related computerized image processing techniques used to analyze images from transmission electron microscopy (TEM). [1] These methods were developed to improve and extend the information obtainable from TEM images of particulate samples, typically proteins or other large biological entities such as viruses .
The particle Reynolds number Re p would be used for particle suspended in flowing fluids, for example. As with flow in pipes, laminar flow typically occurs with lower Reynolds numbers, while turbulent flow and related phenomena, such as vortex shedding , occur with higher Reynolds numbers.
Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene.
A schematic diagram of the structure of laminin 111 and several hypothesized binding sites of cell-surface receptors. [1] Laminin–111 (also "laminin–1") is a protein of the type known as laminin isoforms. It was among the first of the laminin isoforms to be discovered. [2] The "111" identifies the isoform's chain composition of α1β1γ1. [2]