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MilliporeSigma

C3657

Sigma-Aldrich

Human Collagen Type V

from human placenta, powder, suitable for detection assays

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1 MG
$138.00
5 MG
$471.00

$138.00


Estimated to ship onMarch 27, 2025


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1 MG
$138.00
5 MG
$471.00

About This Item

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

$138.00


Estimated to ship onMarch 27, 2025


Request a Bulk Order

Product Name

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

biological source

human placenta

Quality Level

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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This Item
C7521C8374C5608
form

powder

form

powder

form

powder

form

powder

Gene Information

human ... COL5A1(1289)

Gene Information

human ... COL4A2(1284), COL4A3(1285), COL4A4(1286), COL4A5(1287), COL4A6(1288)

Gene Information

human ... COL4A1(1282), COL4A2(1284), COL4A3(1285), COL4A4(1286), COL4A5(1287), COL4A6(1288)

Gene Information

rabbit ... COL1A2(100008997)

impurities

HIV, hepatitis B and hepatitis C, none detected

impurities

HIV, hepatitis B and hepatitis C, none detected

impurities

HIV, hepatitis B and hepatitis C, none detected

impurities

-

solubility

aqueous acid: soluble

solubility

0.5 M acetic acid: 1 mg/mL

solubility

0.5 M acetic acid: 1 mg/mL, clear to very slightly hazy

solubility

aqueous acid: ≤10 mg/mL, aqueous sodium acetate buffer: soluble (0.01-0.5M)

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

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

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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)
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
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 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
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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