C4407
Human Collagen Type III
from human placenta, powder, suitable for cell culture
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| 1 mg | Please contact Customer Service for Availability | $196.00 | |
| 5 mg | Please contact Customer Service for Availability | $615.00 | |
| 25 mg | Please contact Customer Service for Availability | $4,700.00 |
About This Item
Form:
powder
Assay:
≥90% (GE)
Biological source:
human placenta
Product Name
Collagen from human placenta, Bornstein and Traub Type III (Sigma Type X), powder
biological source
human placenta
Quality Level
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.
storage temp.
2-8°C
Gene Information
human ... COL3A1(1300)
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.
1 of 1
This Item | |||
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) - | technique(s) - |
| biological source human placenta | biological source human placenta | biological source human placenta | biological source human placenta |
| 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) | Gene Information human ... COL5A1(1289) | Gene Information human ... COL4A2(1284), COL4A3(1285), COL4A4(1286), COL4A5(1287), COL4A6(1288) |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C4407-25MG | 04061833260999 |
| C4407-5MG | 04061833492130 |
| C4407-1MG | 04061833492123 |