추천 제품
생물학적 소스
bovine pancreas
Quality Level
제품 라인
BioReagent
분석
≥80% (SDS-PAGE)
양식
powder
특이 활성도
≥50 Kunitz units/mg protein
농도
≥60%
기술
cell based assay: suitable
적합성
suitable for molecular biology
응용 분야
cell analysis
외래 활성
protease ≤0.001 units/mg solid
저장 온도
−20°C
SMILES string
[nH]1cncc1CC(NC(=O)CCN)C(=O)O
InChI
1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)
InChI key
CQOVPNPJLQNMDC-UHFFFAOYSA-N
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관련 카테고리
애플리케이션
Ribonuclease B from bovine pancreas is used in the digestion of RNA during cell cycle platform analysis.
생화학적/생리학적 작용
Native RNase BS generated by subtilisin digestion of native RNase B comprising of amino acid residues 21-124 of RNase B, is sensitive to PNGase F digestion. Intramolecular N-glycans of bovine pancreatic RNase B function like chaperone. RNase B is found to be much faster than RNase A, while RNase A is liable to aggregate during regeneration. The stimulatory effect of Asn-oligosaccharide (which corresponds to the most predominant sugar chain of RNase B) reveals that the N-glycans of RNase B facilitates the transformation of bulky intermediates into folded, compact species.
포장
Package size based on protein content
제조 메모
Purified by affinity chromatography
저해제
제품 번호
설명
가격
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
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)
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시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
H Yamaguchi et al.
Journal of biochemistry, 120(3), 474-477 (1996-09-01)
This paper describes a chaperone-like function of the intramolecular N-glycans of bovine pancreatic RNase B. We studied air-oxidative regeneration from reductively denatured species of RNase B and its nonglycosylated form, RNase A. RNase B was reactivated much faster than RNase
Véronique Blanchard et al.
Biochemistry, 47(11), 3435-3446 (2008-02-26)
In glycoanalysis protocols, N-glycans from glycoproteins are most frequently released with peptide- N (4)-( N-acetyl-beta-glucosaminyl)asparagine amidase F (PNGase F). As the enzyme is an amidase, it cleaves the NH-CO linkage between the Asn side chain and the Asn-bound GlcNAc residue.
Audra A Hargett et al.
Molecules (Basel, Switzerland), 26(14) (2021-07-25)
Protein glycosylation is important in many organisms for proper protein folding, signaling, cell adhesion, protein-protein interactions, and immune responses. Thus, effectively determining the extent of glycosylation in glycoprotein therapeutics is crucial. Up to now, characterizing protein glycosylation has been carried
Vijay Ramakrishnan et al.
American journal of hematology, 85(9), 675-686 (2010-07-24)
Interaction of myeloma cells with the bone marrow microenvironment is mediated in large part through different cytokines, especially VEGF and IL6. These cytokines, especially IL6, leads to upregulation of the JAK/STAT pathway in myeloma cell, contributing to increased proliferation, decreased
Yang Xu et al.
iScience, 25(8), 104753-104753 (2022-08-10)
N-Acetylglucosamine (GlcNAc) is an essential monosaccharide required in almost all organisms. Fluorescent labeling of the peptidoglycan (PG) on N-acetylglucosamine has been poorly explored. Here, we report on the labeling of the PG with a bioorthogonal handle on the GlcNAc. We
문서
PNGase Fast denaturing buffer and enzyme provide results similar to a conventional 20-hour protocol, reducing workflow time to about 1 hour.
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