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C3657

Sigma-Aldrich

Human Collagen Type V

from human placenta, powder, suitable for detection assays

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

product name

Collagen from human placenta, Bornstein and Traub Type V (Sigma Type IX), powder

biological source

human placenta

form

powder

impurities

HIV, hepatitis B and hepatitis C, none detected

solubility

aqueous acid: soluble

UniProt accession no.

application(s)

detection

storage temp.

2-8°C

Gene Information

human ... COL5A1(1289)

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Components

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.

Caution

This product should be stored desiccated at -20°C, and will retain activity in these conditions for 3 years.

Preparation Note

This product was prepared by a modification of the pepsin extraction and salt fractionation method of Niyibizi, C., et al., J. Biol. Chem., 259, 14170 (1984). It is an acid soluble collagen that can be dissolved in water with acetic acid added to pH 3.0 (5 mg/mL), yielding an opalescent, colorless solution.

Analysis Note

An SDS polyacrylamide gel electrophoresis test run under reducing conditions consistent with basement membrane collagen yields three major bands.

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Identification of autoantigens and their potential post-translational modification in EGPA and severe eosinophilic asthma.
Esposito, et al.
Frontiers in Immunology, 14, 1164941-1164941 (2023)
Gaoyan G Tang-Siegel et al.
Journal of bacteriology, 204(12), e0021522-e0021522 (2022-12-01)
The human oral pathobiont Aggregatibacter actinomycetemcomitans expresses multiple virulence factors, including the trimeric, extracellular matrix protein adhesin A (EmaA). The posttranslational modification of EmaA is proposed to be dependent on the sugars and enzymes associated with O-polysaccharide (O-PS) synthesis of
Gaoyan Tang et al.
Microbiology (Reading, England), 153(Pt 8), 2447-2457 (2007-07-31)
Adhesion of Aggregatibacter actinomycetemcomitans to extracellular matrix proteins is mediated by antennae-like surface structures composed of EmaA oligomers. EmaA is an outer-membrane protein orthologous to the autotransporter YadA, a virulence determinant of Yersinia. emaA was present in the 27 strains
The serotype a-EmaA adhesin of Aggregatibacter actinomycetemcomitans does not require O-PS synthesis for collagen binding activity.
Tang-Siegel, et al.
Microbiology (Reading, England), 168 (2023)
Di Wen et al.
Protein expression and purification, 171, 105629-105629 (2020-03-24)
Matrix metalloproteinases (MMPs) are evolutionarily conserved extracellular matrix proteinases. Genetic analysis of the Drosophila MMPs, Mmp1 and Mmp2, in vivo reveal that they play vital roles in tissue remodeling. Although the catalytic domain (CD) undertakes most MMP functions, few studies

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