39465
Gelatin from porcine skin
suitable for microbiology, ultrahigh gel strength
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About This Item
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biological source
Porcine
Quality Level
form
powder
quality
ultrahigh gel strength
shelf life
limited shelf life, expiry date on the label
loss
9.5-12.5% loss on drying
transmittance
450 nm, ≥85%
620 nm, ≥95%
pH
5.20-5.60
conductivity
120-190 μS/cm at 30 °C (1%)
viscosity
5.10-5.80 mPa.s
gel strength
280-302 g BloomAOAC
solubility
H2O: 67 mg/mL at 60 °C
cation traces
Ca: ≤100 mg/kg
application(s)
microbiology
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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.
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.
Components
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.
Caution
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.
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 concentrat ion. The Bloom number is proportional to the average molecular mass. Bloom numbers of porcine skin Gelatin vary from 90 to 300 g. Manufactured by Gelita AG
Storage Class Code
11 - Combustible Solids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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M V Nasekin et al.
Anesteziologiia i reanimatologiia, (1)(1), 59-60 (2013-07-03)
The article deals with skills improving problem of epidural anaesthesia with ultrasound control. Methods of gelatin spinal column model making, use and its economical side are discussed in the article.
Johno Breeze et al.
Journal of the Royal Army Medical Corps, 159(2), 84-89 (2013-05-31)
Ballistic gelatin is the most common tissue simulant used to reproduce the penetration of projectiles into muscle but published data to support its use are primarily based on bullets, despite explosive fragments being the most common cause of injury to
Takeo Furuya et al.
The journal of spinal cord medicine, 36(2), 134-139 (2013-07-03)
Besides stimulating angiogenesis or cell survival, basic fibroblast growth factor (bFGF) has the potential for protecting neurons in the injured spinal cord. To investigate the effects of a sustained-release system of bFGF from gelatin hydrogel (GH) in a rat spinal
Monica A Serban et al.
Methods in molecular biology (Clifton, N.J.), 1001, 133-143 (2013-03-16)
Tissue engineering involves the concerted action of biomaterials, cells, and growth factors. Kidney -regeneration relies on the same combination of ingredients. Here, we describe an example of gelatin-based biomaterial preparation and its evaluation in the context of kidney biocompatibility and
Nina E Lamash et al.
PloS one, 8(3), e58433-e58433 (2013-03-19)
Four proteases with molecular masses of 132, 58, 53, and 47 kDa were detected in the digestive system of the holothurian Eupentacta fraudatrix. These proteases displayed the gelatinase activity and characteristics of zinc metalloproteinases. The 58 kDa protease had similar
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