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Key Documents

安全性情報

39465

Millipore

ゼラチン from porcine skin

suitable for microbiology, ultrahigh gel strength

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About This Item

CAS番号:
EC Number:
MDL番号:
UNSPSCコード:
41106212
NACRES:
NA.85

由来生物

Porcine

品質水準

形状

powder

品質

ultrahigh gel strength

シェルフライフ

limited shelf life, expiry date on the label

損失

9.5-12.5% loss on drying

透過率

450 nm, ≥85%
620 nm, ≥95%

pH

5.20-5.60

導電率

120-190 μS/cm at 30 °C (1%)

粘度

5.10-5.80 mPa.s

ゲル強度

280-302 g BloomAOAC

溶解性

H2O: 67 mg/mL at 60 °C

微量陽イオン

Ca: ≤100 mg/kg

アプリケーション

microbiology

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アプリケーション

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.

構成

ゼラチンは、コラーゲン中に存在する平均分子量が大きい水溶性タンパク質の不均一な混合物です。 水中で適切な皮膚、腱、靭帯、骨などを煮沸することでタンパク質が抽出されます。 A型ゼラチンは酸硬化組織由来です。 B型ゼラチンは石灰硬化組織由来です。

注意

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.

調製ノート

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

保管分類コード

11 - Combustible Solids

WGK

nwg

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

39465-500G:
39465-VAR:
39465-BULK:


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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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