C3657
Human Collagen Type IX
from human placenta, powder, suitable for detection assays
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
Quality Level
Gene Information
human ... COL5A1(1289)
Looking for similar products? Visit Product Comparison Guide
Analysis Note
An SDS polyacrylamide gel electrophoresis test run under reducing conditions consistent with basement membrane collagen yields three major bands.
Disclaimer
This product should be stored desiccated at -20°C, and will retain activity in these conditions for 3 years.
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.
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.
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
常规特殊物品
This item has
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.
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
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)
Sarah Finke et al.
Cell surface (Amsterdam, Netherlands), 5, 100032-100032 (2020-08-18)
Cyclic diguanylate (c-di-GMP) signalling affects several cellular processes in Bacillus cereus group bacteria including biofilm formation and motility, and CdgF was previously identified as a diguanylate cyclase promoting biofilm formation in B. thuringiensis. C-di-GMP can exert its function as a
Related Content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service