59625 Results for: "N-Benzylcinchonidinium+chloride&pageNo=36"

Supplier: Apollo Scientific

2,6-Difluoro-4-(trifluoromethyl)phenyl 4-methoxyphenyl ether 95%

Supplier: TCI

1,11-Bis(maleimido)-3,6,9-trioxaundecane ≥98.0% (by HPLC)

Supplier: Apollo Scientific

A mutagenic cogener of PHIP.

Supplier: Apollo Scientific

3-(3,4-Dihydro-4-methyl-3-oxoquinoxalin-2-yl)propanoic acid

Supplier: Apollo Scientific

6-Methyl-3,4-dihydro-2H-pyran-5-carboxylic acid

Supplier: Apollo Scientific

1H,1H-Perfluoro-3,7-dimethyl-1-octanol 97%

Supplier: TCI

3-Nitro-2,6-lutidine ≥98.0% (by GC, titration analysis)

Supplier: Apollo Scientific

(4-Bromo-3,5-dimethyl-1H-pyrazol-1-yl)methanol

Supplier: Apollo Scientific

tert-Butyl-3-(3,4-dichlorobenzyl)-3-formyltetrahydro-1(2H)-pyridinecarboxylate

Supplier: Apollo Scientific

1-(4-Chlorophenyl)-3,5-dimethyl-1H-pyrazole-4-carboxylic acid

Supplier: Apollo Scientific

3,4-Dihydro-2H-1,4-benzoxazine-2-carbonitrile 97%

Supplier: Apollo Scientific

3,4-Difluoro-2-methylphenylboronic acid pinacol ester 95%

Supplier: Apollo Scientific

6,7-Dihydro-4H-thieno[3,2-c]pyran-2-carbaldehyde

Supplier: Apollo Scientific

6,7-Dihydro-4H-thieno[3,2-c]pyran-2-ylmethanol

Supplier: Apollo Scientific

4,6-Dichloro-1H-pyrrolo[3,2-c]pyridine 95%

Supplier: Apollo Scientific

(R)-3,3-Difluoropropane-1,2-diol 98% (85%ee)

Supplier: Apollo Scientific

Ethyl-1H-pyrrolo[3,2-c]pyridine-2-carboxylate 97%

Supplier: Apollo Scientific

4-Chloro-6-methyl-1H-pyrrolo[3,2-c]pyridine 95+%

Supplier: Apollo Scientific

7-Nitro-3,4-dihydro-2H-1,4-benzooxazine 98%

Supplier: Apollo Scientific

tert-Butyl-6-oxo-2-azaspiro[3.3]heptane-2-carboxylate

Supplier: Apollo Scientific

3-Bromo-1-tert-butyl-pyrazolo[3,4-d]pyrimidin-4-ol

Supplier: Avantor Fluid Handling

No need to buy two fitting halves.

Supplier: Apollo Scientific

2-(4-Bromo-2,6-difluorophenyl)-2-methyl-1,3-dioxolane 97%

Supplier: Apollo Scientific

3,4-Dihydro-2H-chromen-3-ylamine hydrochloride 95%

Supplier: Apollo Scientific

3-Amino-6-bromo-8-methyl-3,4-dihydroquinazolin-4-one, tech

Supplier: Apollo Scientific

2-Chloro-1-nitro-3,5-bis(trifluoromethyl)benzene 98%

Supplier: Abcam

Mouse monoclonal [32] to Hemopexin.

Supplier: Bohlender

Spherical ground joint sleeves, made of PTFE, with gripping rings and sealing rings on the outside; seal suitable for high vacuums. Robust design for regular use.

Supplier: Thermo Fisher Scientific

Cobalt ≥99.5% (metals basis), powder 1.6 µm

Supplier: Bioss

Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.