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C4243

Bovine Collagen Type I

2.9-3.2 mg/mL, (Suitable for cell culture and for 3D matrix formation), sterile-filtered

Sinónimos:

Bovine collagen solution, Collagen extract

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Tamaño de envaseSKUDisponibilidadPrecio
20 mL
Comprobar disponibilidad del carrito
US$ 483,00
100 mL
Comprobar disponibilidad del carrito
US$ 1.930,00

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UNSPSC Code:
12352202
NACRES:
NA.75
MDL number:
Biological source:
bovine skin
Form:
liquid
Technique(s):
cell culture | mammalian: suitable (3D matrix formation)
Concentration:
2.9-3.2 mg/mL
Assay:
≥99.9% (SDS-PAGE)

US$ 483,00

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Nombre del producto

Collagen solution from bovine skin, 2.9-3.2 mg/mL, (Suitable for cell culture and for 3D matrix formation), sterile-filtered

biological source

bovine skin

Quality Level

sterility

sterile-filtered

product line

BioReagent

assay

≥99.9% (SDS-PAGE)

form

liquid

packaging

pkg of 100 mL, pkg of 20 mL

concentration

2.9-3.2 mg/mL

technique(s)

cell culture | mammalian: suitable (3D matrix formation)

surface coverage

6‑10 μg/cm2

suitability

gelation test tested

UniProt accession no.

binding specificity

Peptide Source: Fibrinogen

foreign activity

endotoxin ≤1.0 μmole/min-mg protein

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... COL1A1(282187)

General description

Collagen solution is derived by dissolving collagen molecules in an aqueous solution. Collagen type Iα1 (COL1A1) is encoded by the gene that is located on human chromosome 17q21.33. It is the most abundant extracellular matrix (ECM) protein in humans. Type 1 collagen is the major structural protein of bone, tendon, skin and cornea. The encoded protein is a heterotrimer consisting of two α1-chains and one α2-chain.Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.

Application

This highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals
Collagen solution from bovine skin has been used

  • in the preparation of collagen gels.
  • to coat cell culture dishes for HeLa cell line culture.
  • to construct hydrogels laden for HepG2 cell culture.

Biochem/physiol Actions

In 3D environments, cell extensions can use integrins on cell surfaces to activate specific signaling pathways and integran-independent mechanical interactions resulting from the entanglement of matrix fibrils is possible.
Collagen solution from bovine skin is a highly purified solution is suitable for 3-D matrix formation in cell culture. 3-D collagen gels imitate the in vivo cell physiology better than traditional 2D systems and has been proven successful for several cell types including cardian and corneal fibroblasts, depatic stellate cells, and neuroblastoma cells. Such 3-D gels are also useful in studies of mechanotransduction, cell signaling involving the transformation of mechanical signals into biochemical signals. Collagen, type I (COL1A1) participates in fibrosis. COL1A1 is an important component of the connective tissue matrix. [1] It plays a vital role in the growth and maintenance of organ and tissue integrity. This protein also participates in the process of tissue repair.

Preparation Note

This product is prepared from type I bovine collagen purified and extracted from skin and contains a high monomer content. The raw collagen used to prepare this product has been isolated from a closed herd and purified with a GMP manufacturing process that includes inactivation of any possible prion or viral contamination. As supplied, it is a 3 mg/mL aqueous solution in 0.01 M HCl with a pH of 2.0. Collagen denatures when exposed to high temperatures or irradiation. Prior to a pH adjustment, store stock or diluted solutions refrigerated. Following a pH adjustment to 7, solutions should not exceed 40°C and should not be frozen.

Other Notes

Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Be wary of confusing Sigma-type designations with recognized collagen classification types.
Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. As a heterodimer composed of two a1 chains and one a2 chains, it spontaneously forms a triple helix scaffold at neutral pH and 37°C.

Disclaimer

This product ships on wet ice and with recommended storage at 2-8°C, the product will last for 2 years.

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Este artículo
C2124C8919C9791
sterility

sterile-filtered

sterility

sterile-filtered

sterility

aseptically processed

sterility

-

technique(s)

cell culture | mammalian: suitable (3D matrix formation)

technique(s)

cell culture | mammalian: suitable using and for 3D matrix formation.

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

biological source

bovine skin

biological source

bovine skin

biological source

bovine (calf) skin

biological source

bovine (calf) skin

concentration

2.9-3.2 mg/mL

concentration

6 mg/mL

concentration

(0.1% solution in 0.1 M acetic acid)

concentration

-

assay

≥99.9% (SDS-PAGE)

assay

-

assay

-

assay

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


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Artículos

The extracellular matrix (ECM) and its attachment factor components are discussed in this article in relation to their function in structural biology and their availability for in vitro applications.

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.


Oxygen Consumption Characteristics in 3D Constructs Depend on Cell Density
Magliaro C, et al.
Frontiers in Bioengineering and Biotechnology, 7 (2019)
Xin-Hua Liao et al.
Scientific reports, 7, 43639-43639 (2017-03-07)
Hepatocellular carcinoma (HCC) is one of the most prevalent and malignant cancers with high inter- and intra-tumor heterogeneity. A central common signaling mechanism in cancer is proline-directed phosphorylation, which is further regulated by the unique proline isomerase Pin1. Pin1 is
Oxygen Consumption Characteristics in 3D Constructs Depend on Cell Density
Chiara Magliaro, et al.
Frontiers in Bioengineering and Biotechnology, 7, 251-251 (2019)



Número de artículo de comercio global

SKUGTIN
C4243-100ML04061833491850
C4243-20ML04061833491867

Questions

1–2 of 2 Questions  
  1. What does the "Other Notes" statement in the product description mean when it cautions against confusing Sigma-type designations with recognized collagen classification types?

    1 answer
    1. The product C4243 is a sterile-filtered bovine skin collagen solution suitable for cell culture. It is prepared from type I bovine collagen, following the nomenclature proposed by Bornstein and Traub.

      The caution regarding the confusion of Sigma-type designations with recognized collagen classification types refers to specific examples such as Cat # C3657, which is listed as (Sigma Type IX) but is actually Collagen from human placenta Bornstein and Traub Type V, based on literature-based classification. Type IX is an internal classification used by Sigma.

      Helpful?

  2. Does diluting C4243, a 3mg/ml collagen solution, to 0.03mg/ml will result in gel formation at room temperature?

    Does diluting C4243, a 3mg/ml collagen solution, to 0.03mg/ml will result in gel formation at room temperature?

    1 answer
    1. The laboratory has not conducted characterization of this product. In the literature linked below, when testing the stiffness of collagen gels, a noticeable decrease in stiffness corresponds with a reduction in collagen concentration to as low as 0.4 mg/mL. Given that 0.03 mg/mL represents a concentration more than ten times lower, it is unlikely that gel formation at this concentration would be practically applicable.

      For further reading on the subject, the following publication might be useful: "Effect of collagen gel stiffness on neurite extension", J Biomater Sci Polym Ed. 2004;15(12):1521-31. doi: 10.1163/1568562042459698. https://pubmed.ncbi.nlm.nih.gov/15696797/

      Helpful?

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