추천 제품
생물학적 소스
human lung
Quality Level
형태
lyophilized powder
불순물
salt, free
solubility
H2O: >10 mg/mL (more soluble at pH>7)
UniProt 수납 번호
저장 온도
2-8°C
InChI
1S/C27H48N6O6/c1-9-17(6)23(32-24(36)19(13-15(2)3)30-18(7)34)26(38)29-14-21(35)31-22(16(4)5)27(39)33-12-10-11-20(33)25(37)28-8/h15-17,19-20,22-23H,9-14H2,1-8H3,(H,28,37)(H,29,38)(H,30,34)(H,31,35)(H,32,36)/t17-,19-,20-,22-,23-/m0/s1
InChI key
DPUYCSDGMSDKKV-MKBYFEBXSA-N
유전자 정보
human ... ELN(2006)
애플리케이션
Elastin is a structural protein which has been used in studies of chronic obstructive pulmonary disease (COPD). It may be used to investigate why there is a lack of repair for these proteins in patients with COPD.
제조 메모
Prepared from E7152 using the method of Partrige, et al.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastin.
The Biochemical journal, 61(1), 11-21 (1955-09-01)
Respiratory research, 9, 41-41 (2008-05-20)
COPD is characterised by loss of alveolar elastic fibers and by lack of effective repair. Elastic fibers are assembled at cell surfaces by elastin binding protein (EBP), a molecular chaperone whose function can be reversibility inhibited by chondroitin sulphate of
Pro-inflammatory phenotype of COPD fibroblasts not compatible with repair in COPD lung.
Journal of Cellular and Molecular Medicine (2011)
Journal of the American Chemical Society, 135(9), 3675-3679 (2013-02-07)
The chimeric proteins, silk-elastin-like protein polymers (SELPs), consist of repeating units of silk and elastin to retain the mechanical strength of silk, while incorporating the dynamic environmental sensitivity of elastin. A retinal-modified SELP was prepared, modified, and studied for photodynamic
PloS one, 8(2), e56136-e56136 (2013-02-15)
Many cardiac diseases have been associated with increased fibrosis and changes in the organization of fibrillar collagen. The degree of fibrosis is routinely analyzed with invasive histological and immunohistochemical methods, giving a limited and qualitative understanding of the tissue's morphological
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