C3657
Human Collagen Type IX
from human placenta, powder, suitable for detection assays
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この商品について
Form:
powder
Biological source:
human placenta
製品名
コラーゲン ヒト胎盤由来, 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)
Preparation Note
Niyibizi, C., et al., J. Biol. Chem., 259, 14170(1984)におけるペプシン抽出と塩分画法を改変して調製しています。
Analysis Note
An SDS polyacrylamide gel electrophoresis test run under reducing conditions consistent with basement membrane collagen yields three major bands.
Other Notes
コラーゲンは複数の構造的および遺伝的に異なるタイプに分類されています。弊社ではBornsteinとTraubが提唱した命名法を使用しています。シグマ アルドリッチのタイプ分けは一般的なコラーゲン分類とは異なりますのでご注意ください。
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.
Disclaimer
This product should be stored desiccated at -20°C, and will retain activity in these conditions for 3 years.
保管分類
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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)
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