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Sigma-Aldrich

Human Collagen Type I

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

Synonym(s):

Human Collagen

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About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.75

product name

Human Collagen Type I,

biological source

human

Quality Level

Assay

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

form

liquid

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)

solubility

water: soluble at 20 °C

NCBI accession no.

UniProt accession no.

Binding Specificity

Peptide Source: Elastin

Peptide Source: Fibronectin

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... COL1A1(1277)

Related Categories

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
  • as a protein standard in histological analysis of lung tissue samples, providing a reference for the composition and characterization of extracellular matrix (ECM) components

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Whole exome sequencing reveals a mutation in an osteogenesis imperfecta patient
Ergun MA, et al.
Meta Gene (2017)
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
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)
Signal inhibitory receptor on leukocytes-1 recognizes bacterial and endogenous amphipathic ?-helical peptides
Rumpret M, et al.
Faseb Journal (2021)
Yongsheng Gao et al.
Science advances, 6(31), eaba0588-eaba0588 (2020-08-11)
Uncontrolled noncompressible hemorrhage is a major cause of mortality following traumatic injuries in civilian and military populations. An injectable hemostat for point-of-care treatment of noncompressible hemorrhage represents an urgent medical need. Here, we describe an injectable hemostatic agent via polymer

Articles

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

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

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

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

Protocols

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

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