Skip to Content
Merck
All Photos(3)

Key Documents

48722

Millipore

Gelatin from porcine skin

medium gel strength, suitable for microbiology

Synonym(s):

Gelatine, hydrolyzed collagen, collagen hydrolysate, gelatine hydrolysate

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
41106212
NACRES:
NA.85

biological source

Porcine

Quality Level

sterility

non-sterile

form

powder

quality

medium gel strength

packaging

bottle of 100 g
bottle of 500 g

ign. residue

≤2%

loss

≤15% loss on drying

color

light yellow

pH

4.0-6.0 (25 °C, 67 mg/mL in H2O)

gel strength

165-195 g Bloom (67 mg/ml water)

solubility

H2O: 67 mg/mL at 50 °C, slightly hazy, slightly yellow

anion traces

chloride (Cl-): ≤3000 mg/kg

cation traces

Ca: ≤2000 mg/kg
Cd: ≤5 mg/kg
Co: ≤5 mg/kg
Cr: ≤10 mg/kg
Cu: ≤50 mg/kg
Fe: ≤50 mg/kg
K: ≤500 mg/kg
Mg: ≤500 mg/kg
Mn: ≤5 mg/kg
Na: ≤5000 mg/kg
Ni: ≤5 mg/kg
Pb: ≤5 mg/kg
Zn: ≤10 mg/kg

application(s)

microbiology

Looking for similar products? Visit Product Comparison Guide

General description

Gelatin from porcine skin is generated from the acidic digestion of collagen and is referred to as type A. It is a hydrocolloid and is rich in glycine, proline, and hydroxyproline, which impart structural stability. It is synthesized from the alkaline digestion of collagen from porcine. Gelatin takes up a random coil structure after digestion from the triple helical collagen.

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, and Type B from lime-cured tissue.

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. This product has a gel strength of 180.

Application

Gelatin has been used in many applications, such as in coating cell culture plates to improve attachment of cells, in 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.

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. Manufactured by Gelita AG

Storage Class Code

11 - Combustible Solids

WGK

nwg

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Bin Liu et al.
Materials science & engineering. C, Materials for biological applications, 112, 110905-110905 (2020-05-16)
Three-dimensional (3D) bioprinting is an extremely convenient biofabrication technique for creating biomimetic tissue-engineered bone constructs and has promising applications in regenerative medicine. However, existing bioinks have shown low mechanical strength, poor osteoinductive ability, and lacking a suitable microenvironment for laden
Gelatin Liquefaction by Bacteria.
M Levine et al.
Journal of bacteriology, 8(4), 297-306 (1923-07-01)
Leslie Crews et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 28(16), 4250-4260 (2008-04-18)
Altered expression and mutations in alpha-synuclein (alpha-syn) have been linked to Parkinson's disease (PD) and related disorders. The neurological alterations in PD patients have been associated with degeneration of dopaminergic cells and other neuronal populations. Moreover, recent studies in murine
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.
Louise Clemmesen et al.
Ugeskrift for laeger, 175(9), 576-578 (2013-04-24)
This article describes the production of a low-cost training phantom for ultrasound guided invasive procedures of peripheral and central veins and presents a video of the process. The phantom can be adapted for use with other ultrasound techniques. It is

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