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C9879

Sigma-Aldrich

Bovine Collagen Type I

from bovine achilles tendon, powder, suitable for substrate for collagenase

别名:

Collagen powder

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About This Item

CAS号:
9007-34-5
EC 号:
232-697-4
MDL编号:
MFCD00130825
UNSPSC代码:
12352202
NACRES:
NA.61

product name

胶原 来源于牛跟腱, powder, suitable for substrate for collagenase

生物来源

bovine Achilles tendon

质量水平

200

形式

powder

技术

ELISA: suitable
activity assay: suitable

适用性

suitable for substrate for collagenase

UniProt登记号

P02459

储存温度

2-8°C

基因信息

bovine ... COL2A1(407142)

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一般描述

胶原是体内广泛表达的蛋白。人体组织中有20种不同类型的胶原蛋白。I型胶原是丰富的骨蛋白。它构成了约90%的骨有机物。
使用Bornstein和Traub命名的胶原蛋白术语源自参考文献；Bornstein, P. and Traub, W. The Proteins, (1979) 4, 411-605
胶原蛋白被分为许多种结构和遗传性不同的类型。我们使用Bornstein和Traub提出的命名法。不要混淆Sigma分类标识和公认的胶原蛋白分类类型。

应用

来自牛跟腱的胶原适合用于：
  • 胶原酶活性的检测
  • 作为使用差示扫描量热法，热重法，气相色谱法和傅里叶变换红外光谱法进行人体骨骼热分析研究中的参考样品
  • 作为开发用于确定体外胶原降解的简单测定的底物
  • 固相酶联免疫吸附试验检测整合糖蛋白二肽基肽酶IV与不溶性I型胶原结合活性的研究
来自牛跟腱的胶原是天然存在的蛋白，呈细长的原纤维形式。它可用于纤维软骨区的研究，胶原蛋白在插入跟骨之前必须首先穿过纤维软骨区。它也可用于研究生长因子对跟腱愈合过程中胶原含量和交联的影响。
牛跟腱胶原蛋白用于植物提取物的研究中，作为MMP-胶原酶的抑制剂，MMP-胶原酶是骨关节炎和类风湿关节炎中软骨分解的推定活性剂。

生化/生理作用

来自牛跟腱的胶原是天然存在的蛋白，呈细长的原纤维形式。它可用于纤维软骨区的研究，胶原蛋白在插入跟骨之前必须首先穿过纤维软骨区。它也可用于研究生长因子对跟腱愈合过程中胶原含量和交联的影响。
胶原是一种不溶性纤维蛋白，是细胞外基质和结缔组织的一部分。它负责组织承受拉伸的能力。 称为前胶原的长前体在ER中合成和组装，分泌到细胞外空间并加工形成胶原纤维。不同类型的胶原蛋白由包含三个多肽链的分子组成，这些多肽链以三重螺旋构象排列，氨基酸序列略有不同。一级结构是在每三个位置具有甘氨酸的重复基序，经常在脯氨酸或4-羟脯氨酸残基之前。

制备说明

根据Einbinder, J. and Schubert, M., J. Biol. Chem., 188, 335 (1951)中的方法制备。

重悬

本品为不溶性胶原制剂。它不溶于水，水性缓冲液，稀酸和有机溶剂。为了在胶原酶测定中用作底物，该胶原可以制备为在含0.36 mM氯化钙的50mM TES缓冲液（pH值7.4）中的混悬液。

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

分析证书(COA)

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. How should Product No. C9879, Collagen from bovine, be reconstituted?

    This product is an insoluble collagen preparation. It is insoluble in water, aqueous buffers, dilute acid, and organic solvents. A suspension can be prepared in 50 mM TES buffer, pH 7.4 with 0.36 mM calcium chloride, but not a clear solution.

  6. What application can Product No. C9879, Collagen from bovine, be used in?

    This product is suitable for use as a substrate for collagenase. It is not suitable for use as an attachment factor in coating glassware.

  7. What is the structure of the Collagen from bovine - C9879?

    The amino acid sequence of the primary structure is mainly a repeating motif with glycine in every third position, and a proline or 4-hydroxyproline frequently preceding the glycine residue.

  8. What is the molecular weight of product C9879, Collagen from bovine achilles tendon?

    Since product C9879 is an insoluble collagen preparation, it is difficult to make any kind of molecular weight determination.  However, based on the reported structure of this collagen, the expected molecular weight would be approximately 300 kDa.

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

Extraction and partial characterization of collagen from different animal skins
Quereshi S, et al.
Recent Research in Science and Technology, 2(9) (2010)
M L Tanzer
Science (New York, N.Y.), 180(4086), 561-566 (1973-05-11)
The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is
Thermal analysis study of human bone
Lozano L F, et al.
J. Mater. Sci., 38, 4777-4782 (2003)
Structurally distinct collagen types.
P Bornstein et al.
Annual review of biochemistry, 49, 957-1003 (1980-01-01)
Bradley E Layton et al.
Journal of molecular evolution, 66(6), 539-554 (2008-06-04)
Two competing effects at two vastly different scales may explain collagen's current translation length. The necessity to have long molecules for maintaining mechanical integrity at the organism and supraorganism scales may be limited by the need to have small molecules
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