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Human Collagen Type I

from human placenta, liquid, 1 mg/mL, suitable for cell culture, used for gel formation

Synonim(y):

Human Collagen

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Informacje o tej pozycji

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.75
Biological source:
human
Form:
liquid, solution
Technique(s):
cell culture | mammalian: suitable
Concentration:
1 mg/mL
Assay:
>90% (collagen type I, SDS-PAGE)
Informacje o cenach i dostępności nie są obecnie dostępne.
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Nazwa produktu

Human Collagen Type I, 1 mg/mL, solution, BioReagent, suitable for cell culture

biological source

human

Quality Level

assay

>90% (collagen type I, SDS-PAGE)

form

liquid, solution

manufacturer/tradename

Chemicon®

concentration

1 mg/mL

technique(s)

cell culture | mammalian: suitable

impurities

<1% collagen type II,IV-VI & non-collagen proteins., <10% collagen type III

input

sample type pancreatic stem cell(s)
sample type mesenchymal stem cell(s)
sample type epithelial cells
sample type induced pluripotent stem cell(s)
sample type neural stem cell(s)
sample type: human embryonic stem cell(s)
sample type hematopoietic stem cell(s)

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Ta pozycja
CC052CC076C6745
technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

biological source

human

biological source

human

biological source

human

biological source

human cell culture

concentration

1 mg/mL

concentration

1 mg/mL

concentration

1 mg/mL

concentration

0.3 mg/mL

assay

>90% (collagen type I, SDS-PAGE)

assay

90% (Human collagen type II)

assay

95% (Human collagen type IV, SDS-PAGE)

assay

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

form

liquid, solution

form

liquid, solution

form

liquid, solution

form

solution

General description

Human type I collagen is purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of a pepsin extraction of human placenta. Collagen is a major structural protein found in connective tissues such as skin, tendon, cartilage, ligaments, bone, the part of the eyeball that is white (sclera), and the spaces between cells and tissues called the extracellular matrix. It imparts structure and strength to the connective tissues. The gene for collagen type I alpha 1 (COL1A1) is mapped to human chromosome 17q21.33.Type I collagen is initially produced as procollagen in cells. This protein consists of two pro-alpha1(I) protein strands combined with a pro-alpha2(I) procollagen strand that form a triple-stranded rope-like structure. While in the cell, enzymes modify certain amino acids in the protein (lysine and proline) by adding chemical groups that are necessary for the three strands to form stable molecules and make connections (cross-links) between chains. Other enzymes add sugars to the protein. Now complete, the triple-stranded type I procollagen molecule leaves the cell and is processed by enzymes that clip small segments off both ends. The procollagen molecules arrange themselves into long, thin fibrils outside of the cell. The fibrils come together in side-by-side groups to form collagen fibers. Cross-linking between molecules in fibrils produces a very stable protein structure, which contributes to collagen tissue strengthening function.

Application

Human Collagen Type I has been used:
  • as a control in the 2B4 nuclear factor of activated T-cells (NFAT)–GFP reporter cell assay, where its interaction with reporter cells can be evaluated for nuclear factor of activated T-cells (NFAT) promoter-driven GFP expression
  • for coating glass slides in dynamic binding assays to create a substrate for the specific binding and study of platelets and conjugates in flow channels[1]
  • as a protein standard in histological analysis of lung tissue samples, providing a reference for the composition and characterization of extracellular matrix (ECM) components[2]

Biochem/physiol Actions

Mutations in the collagen type I alpha 1 (COL1A1) gene are associated with osteogenesis imperfecta types I–IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis.

Physical form

Purified protein. Liquid containing 0.5 M Acetic acid, pH 2.5. Can be diluted in PBS for applications.

Analysis Note

Purity was controlled by SDS-PAGE and reaction with anti-collagen type-specific antibodies

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
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Klasa składowania

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Signal inhibitory receptor on leukocytes-1 recognizes bacterial and endogenous amphipathic ?-helical peptides
Rumpret M, et al.
Faseb Journal (2021)
Whole exome sequencing reveals a mutation in an osteogenesis imperfecta patient
Ergun MA, et al.
Meta Gene (2017)
A 235 Kb deletion at 17q21.33 encompassing the COL1A1, and two additional secondary copy number variants in an infant with type I osteogenesis imperfecta: A rare case report
Numbere N, et al.
Molecular Genetics & Genomic Medicine (2020)
Physicochemical characterization and molecular organization of the collagen A and B chains.
R K Rhodes et al.
Biochemistry, 17(17), 3442-3448 (1978-08-22)
Karolina Chrabaszcz et al.
Cancers, 13(2) (2021-01-10)
The current understanding of mechanisms underlying the formation of metastatic tumors has required multi-parametric methods. The tissue micro-environment in secondary organs is not easily evaluated due to complex interpretation with existing tools. Here, we demonstrate the detection of structural modifications

Produkty

Białka macierzy zewnątrzkomórkowej, takie jak laminina, kolagen i fibronektyna, mogą być stosowane jako podłoża do mocowania komórek w hodowli komórkowej.

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

Protokoły

Ta strona obejmuje protokoły powlekania ECM opracowane dla czterech rodzajów ECM na wkładkach Millicell®-CM, kolagenu typu 1, fibronektyny, lamininy i matrigelu.

This page covers the ECM coating protocols developed for four types of ECMs on Millicell®-CM inserts, Collagen Type 1, Fibronectin, Laminin, and Matrigel.

Powiązane treści

As the focus of stem cell research undergoes a transition from animal to human models, researchers are in critical need of validated products to support the isolation, maintenance, differentiation, and characterization of human stem cells. While many reagents designed for rodent systems can be applied to human stem cell studies, they are not truly optimized for robust human stem cell culture or analysis. This is why human stem cell researchers have always trusted EMD Millipore, the first provider of commercially available human embryonic stem cells and human neural stem cell lines, to accelerate their research. All of our human stem cell systems are extensively tested in defined media culture, and differentiated progeny are comprehensively characterized with highly validated antibodies and detection reagents.

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