C4407

Human Collagen Type III

Name: Human Collagen Type III
Brand: SIGMA

from human placenta, powder, suitable for cell culture

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About This Item

CAS Number:

9007-34-5

EC Number:

232-697-4

MDL number:

MFCD00130825

UNSPSC Code:

12352202

NACRES:

NA.32

Key Documents

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Product Name

Collagen from human placenta, Bornstein and Traub Type III (Sigma Type X), powder

biological source

human placenta

Quality Level

200

Assay

≥90% (GE)

form

powder

technique(s)

cell culture | mammalian: suitable

impurities

HIV, hepatitis B and hepatitis C, none detected

solubility

aqueous acid: soluble

UniProt accession no.

Q03692

storage temp.

2-8°C

Gene Information

human ... COL3A1(1300)

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This Item	C7774	C1188	C7806
Sigma-Aldrich C4407 Collagen from human placenta	Sigma-Aldrich C7774 Collagen from human placenta	Sigma-Aldrich C1188 Collagen from bovine tracheal cartilage	Sigma-Aldrich C7806 Collagen from bovine nasal septum
technique(s) cell culture \| mammalian: suitable	technique(s) cell culture \| mammalian: suitable	technique(s) -	technique(s) ELISA: suitable
biological source human placenta	biological source human placenta	biological source bovine cartilage (tracheal)	biological source bovine nasal septum
assay ≥90% (GE)	assay -	assay -	assay -
form powder	form powder	form powder	form powder
Gene Information human ... COL3A1(1300)	Gene Information bovine ... CSN2(281099), CSN3(281728) human ... COL4A3(1285), COL4A4(1286), COL4A6(1288)	Gene Information cow ... COL2A1(407142)	Gene Information bovine ... COL2A1(407142)
solubility aqueous acid: soluble	solubility -	solubility aqueous acid: soluble	solubility aqueous acid: soluble

Application

Collagen from human placenta has been used to assess the bioelectric effects of quinine on airway epithelial cells, to study the selective toxicity of engineered lentvirus lytic peptides and in a particle aggregation assay for the rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus. It has also been used in a magnesium-dependent, collagen-binding assay during characterization of human lung tumor-associated antigens.

Preparation Note

This product was prepared by a modification of the pepsin extraction and salt fractionation method of Hill, R.J. and Harper, E., Anal. Biochem., 141 (1984). It is a lyophilized powder that can be reconstituted in sterile .5 M acetic acid, PBS or water at 1 mg/mL. A PBS solution will be stable for at least one year at -20°C.

Analysis Note

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

Other Notes

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.

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.

Disclaimer

This product should be stored at 2-8 °C and will retain activity in these conditions for 2 years.

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

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Protein C or Protein S deficiency associates with paradoxically impaired platelet-dependent thrombus and fibrin formation under flow.

Sanne L N Brouns et al.

Research and practice in thrombosis and haemostasis, 6(2), e12678-e12678 (2022-03-15)

Low plasma levels of protein C or protein S are associated with venous thromboembolism rather than myocardial infarction. The high coagulant activity in patients with thrombophilia with a (familial) defect in protein C or S is explained by defective protein

Structure-Based Cyclic Glycoprotein Ibα-Derived Peptides Interfering with von Willebrand Factor-Binding, Affecting Platelet Aggregation under Shear.

Johana Hrdinova et al.

International journal of molecular sciences, 23(4) (2022-02-27)

The plasmatic von Willebrand factor (VWF) circulates in a compact form unable to bind platelets. Upon shear stress, the VWF A1 domain is exposed, allowing VWF-binding to platelet glycoprotein Ib-V-IX (GPIbα chain). For a better understanding of the role of

Investigating the morphological, mechanical and degradation properties of scaffolds comprising collagen, gelatin and elastin for use in soft tissue engineering.

Chloe N Grover et al.

Journal of the mechanical behavior of biomedical materials, 10, 62-74 (2012-04-24)

Collagen-based scaffolds can be used to mimic the extracellular matrix (ECM) of soft tissues and provide support during tissue regeneration. To better match the native ECM composition and mechanical properties as well as tailor the degradation resistance and available cell

Platelet-primed interactions of coagulation and anticoagulation pathways in flow-dependent thrombus formation.

Sanne L N Brouns et al.

Scientific reports, 10(1), 11910-11910 (2020-07-19)

In haemostasis and thrombosis, platelet, coagulation and anticoagulation pathways act together to produce fibrin-containing thrombi. We developed a microspot-based technique, in which we assessed platelet adhesion, platelet activation, thrombus structure and fibrin clot formation in real time using flowing whole

Involvement of von Willebrand factor and botrocetin in the thrombocytopenia induced by Bothrops jararaca snake venom.

Camila Martos Thomazini et al.

PLoS neglected tropical diseases, 15(9), e0009715-e0009715 (2021-09-04)

Patients bitten by snakes consistently manifest a bleeding tendency, in which thrombocytopenia, consumption coagulopathy, mucous bleeding, and, more rarely, thrombotic microangiopathy, are observed. Von Willebrand factor (VWF) is required for primary hemostasis, and some venom proteins, such as botrocetin (a

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