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Merck
모든 사진(4)

문서

C9791

Sigma-Aldrich

Bovine Collagen Type I

from bovine skin, powder, suitable for cell culture

동의어(들):

Type I collagen

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC 코드:
12352202
NACRES:
NA.75

product name

Collagen from calf skin, Bornstein and Traub Type I, solid, BioReagent, suitable for cell culture

생물학적 소스

bovine (calf) skin

제품 라인

BioReagent

형태

solid

포장

poly bottle of 10 mg
poly bottle of 100 mg
poly bottle of 250 mg
poly bottle of 50 mg

기술

cell culture | mammalian: suitable

표면 범위

6‑10 μg/cm2

solubility

0.1 M acetic acid: 1 mg/mL (Allow to stir at room temperature 1-3 hours until dissolved.)

UniProt 수납 번호

결합 특이성

Peptide Source: Fibronectin

Peptide Source: Laminin

배송 상태

ambient

저장 온도

2-8°C

유전자 정보

bovine ... COL1A1(282187)

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관련 카테고리

일반 설명

All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. Collagen type I is a component of skin, bone, tendon, and other fibrous connective tissues. It is a left handed helix with three polypeptide chains and contains repeating units of glycine, proline and hydroxyproline amino acids. It is a component of extracellular matrix and close to 28 types is present in bovine.

애플리케이션

Collagen from calf skin has been used:
  • as a component of collagen gel matrix for culturing preantral follicles
  • as a component of Roswell Park Memorial Institute, for culturing gilthead seabream kidney leukocytes and macrophages and acidophilic granulocytes
  • to coat transwells prior to seeding of epithelial cell culture

This product is intended to produce thin layer coatings on tissue culture plates to facilitate attachment of anchorage-dependent cells, recommended for use at 6-10 μg/cm2. It is NOT intended for production of 3-D gels. Type I collagen is often used in cell culture as an attachment substratum with myoblasts, spinal ganglia, hepatocytes, embryonic lung, heart explants, fibroblasts, endothelial cells, and islet cells have all been cultured successfully on films or gels of type I collagen. Collagen type I may also be used in research of Idiopathic pulmonary fibrosis (IPF), studies on the effect of ER stress IPF on lung fibroblasts. Collagen in acidic solution can produce three dimensional scaffolding with use in bioengineering and cell culture applications.

생화학적/생리학적 작용

Collagen from calf skin is intended to produce thin layer coatings on tissue culture plates to facilitate attachment of anchorage-dependent cells, recommended for use at 6-10 μg/cm2. It is NOT intended for production of 3-D gels. Type I collagen is often used in cell culture as an attachment substratum with myoblasts, spinal ganglia, hepatocytes, embryonic lung, heart explants, fibroblasts, endothelial cells, and islet cells have all been cultured successfully on films or gels of type I collagen. Collagen type I may also be used in research of Idiopathic pulmonary fibrosis (IPF), studies on the effect of ER stress IPF on lung fibroblasts. Collagen in acidic solution can produce three dimensional scaffolding with use in bioengineering and cell culture applications. Mutations in collagen encoding proteins are implicated cattle diseases. Collagen type I on heat denaturation results in disruption of triple helix to a randomly coils. It has applications in food and cosmetics and is used as biomaterial in in tissue engineering.

성분

All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition.

제조 메모

This product was prepared by a modification of Gallop, P.M. and Seifter, S., Meth. Enzymol., VI, 635 (1963). It is soluble at 1 mg/mL in .1 M acetic acid and should be stirred at room temperature for 1-3 hours until dissolved.

기타 정보

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Survival and developmental competence of buffalo preantral follicles using three-dimensional collagen gel culture system
Sharma GT, et al.
Animal Reproduction Science, 114(1-3), 115-124 (2009)
Collagen regulates the activation of professional phagocytes of the teleost fish gilthead seabream
Castillo-Briceno P, et al.
Molecular Immunology, 46(7), 1409-1415 (2009)
D Warnecke et al.
Osteoarthritis and cartilage, 28(11), 1482-1491 (2020-08-03)
Because the literature relating to the influence of degeneration on the viscoelasticity and tissue composition of human lateral menisci remains contradictory or completely lacking, the aim of this study was to fill these gaps by comprehensively characterising the biomechanical properties
Krister Gjestvang Grønlien et al.
International journal of biological macromolecules, 156, 394-402 (2020-04-15)
Natural deep eutectic solvents (NADES) have previously shown antibacterial properties alone or in combination with photosensitizers and light. In this study, we investigated the behavior of the structural protein collagen in a NADES solution. A combination of collagen and NADES
Isolation and air-liquid interface culture of human large airway and bronchiolar epithelial cells
Bals R, et al.
Journal of Cystic Fibrosis : Official Journal of the European Cystic Fibrosis Society, 3, 49-51 (2004)

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