G8150
Gelatin from porcine skin
suitable for electrophoresis, Type A
biological source
Porcine skin
type
Type A
Assay
70-90% protein basis (biuret)
form
powder
technique(s)
ELISA: suitable
cell culture | mammalian: suitable
electrophoresis: suitable
immunocytochemistry: suitable
western blot: suitable
gel strength
~300 g Bloom
foreign activity
Protease, none detected
Looking for similar products? Visit Product Comparison Guide
Application
This product is recommended for use as a cell culture substratum at 1-5 μg/cm2 or 0.5-50 μg/mL.  The optimal concentration does depend on cell type as well as the application and research objectives.  Gelatin has been used in many applications.  It has use in coating cell culture to improve attachment of cells, being added to PCR to stabilize Taq DNA, as a blocking reagent in Western blotting, ELISA, and immunochemistry, and as a component of media for species differentiation in bacteriology.  As a biocompatible polymer, it has used as a delivery vehicle for release of active biomolecules and in generation of scaffolds for tissue engineering applications. In the pharmaceutical industry, geltan can be used as a suspending and encapsulating agent, among other applications.
Preparation Note
This product is derived from porcine skin. Gelatin is soluble in hot than in cold water.  It is practically insoluble in most organic solvents such as alcohol, chloroform, carbon disulfide, carbon tetrachloride, ether, benzene, acetone, and oils.  The Bloom number, determined by the Bloom gelometer, is an indication of the strength of a gel formed from a solution of the known concentration.  The Bloom number is proportional to the average molecular mass.  Bloom numbers of porcine skin Gelatin vary from 90 to 300 g. Suitable for use as a blocking reagent for Western blots.
Other Notes
Gelatin is a heterogeneous mixture of water-soluble proteins of high average molecular masses, present in collagen.  Proteins are extracted by boiling the relevant skin, tendons, ligaments, bones, etc. in water.  Type A gelatin is derived from acid-cured tissue.  Type B is derived from lime-cured tissue.
Disclaimer
Dry gelatin, when stored in airtight containers at room temperature, will remain unchanged for many years.  When heated at 100°C in the presence of air, it swells becomes soft and disintegrates to a carbonaceous mass with evolution of pyridine bases and ammonia
Storage Class Code
13 - Non Combustible Solids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
J C Vidal-Quist et al.
Medical and veterinary entomology, 31(3), 272-280 (2017-04-22)
Products manufactured from mass-cultured house dust mites, currently commercialized for the diagnosis and immunotherapy of allergy, are heterogeneous in terms of allergen composition and thus present concerns to regulatory authorities. The most abundant species, Dermatophagoides pteronyssinus (Trouessart) (Astigmata: Pyroglyphidae), produces
Martín Donato et al.
Experimental physiology, 95(2), 274-281 (2009-11-03)
The activation of matrix metalloproteinases (MMPs) contributes to myocardial injury at the onset of reperfusion; however, their role in ischaemic postconditioning is unknown. The aim of the present study was to examine the effects of ischaemic postconditioning on MMP activity
Akikazu Fujita et al.
Nature protocols, 5(4), 661-669 (2010-04-03)
An important goal of membrane biology is to define the local heterogeneity of membrane lipid composition. Here we describe a quantitative electron microscopic method that enables the localization of specific membrane lipids at the nanometer scale. The method involves freezing
Andrej Roczkowsky et al.
Cardiovascular research, 116(5), 1021-1031 (2019-08-03)
Matrix metalloproteinase-2 (MMP-2) is a zinc-dependent protease which contributes to cardiac contractile dysfunction when activated during myocardial ischaemia-reperfusion (IR) injury. MMP-2 is localized to several subcellular sites inside cardiac myocytes; however, its role in the sarcoplasmic reticulum (SR) is unknown.
Guizhen Zhao et al.
Circulation research, 121(12), 1331-1345 (2017-11-02)
Although not fully understood, the phenotypic transition of vascular smooth muscle cells exhibits at the early onset of the pathology of aortic aneurysms. Exploring the key regulators that are responsible for maintaining the contractile phenotype of vascular smooth muscle cells
Related Content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service