Supplier:
Bon Opus Biosciences
Description:
Bon Opus Biosciences offers quality recombinant proteins products covering a broad collection of cytokines, enzymes, diagnostic and detection reagents, and other protein-related products
Catalog Number:
(89161-632)
Supplier:
Enzo Life Sciences
Description:
Potent and selective irreversible cell permeable cathepsin B inhibitor. Methyl ester (Me) is hydrolyzed by intracellular esterases releasing the active inhibitor. Prevents death of CA1 neurons after ischemia following IV delivery after the ischemic insult. In isolated rat osteoclasts it inhibited bone resorption with a maximal effect at 50 µM. This product is only suitable for in vivo and whole cell experiments. The free acid form must be used for in vitro experiments. Can be used to discriminate between cathepsin B and L/S forms.
Catalog Number:
(76108-308)
Supplier:
Bioss
Description:
Golgi auto-antigen; probably involved in maintaining cis-Golgi structure.
Catalog Number:
(TCE0798-25G)
Supplier:
TCI America
Description:
CAS Number: 121-39-1
MDL Number: MFCD00005123 Molecular Formula: C11H12O3 Molecular Weight: 192.21 Purity/Analysis Method: >90.0% (GC) Form: Clear Liquid Boiling point (°C): 152 Flash Point (°C): 113 Specific Gravity (20/20): 1.13 Specific rotation [a]20/D: 0 deg (neat) Storage Temperature: 0-10°C
Catalog Number:
(10335-044)
Supplier:
Bioss
Description:
Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges.
Supplier:
AGILENT TECHNOLOGIES, INC (CSD)
Description:
Ideal for separations of cis- and trans-fatty acid methyl esters in food testing applications.
Catalog Number:
(10396-730)
Supplier:
Bioss
Description:
VAPA is a type IV membrane protein, present in the plasma membrane, intracellular vesicles and may also be associated with the cytoskeleton. This protein may function in vesicle trafficking, membrane fusion, protein complex assembly and cell motility. Two transcript variants encoding distinct isoforms have been identified.
Catalog Number:
(10396-722)
Supplier:
Bioss
Description:
VAPA is a type IV membrane protein, present in the plasma membrane, intracellular vesicles and may also be associated with the cytoskeleton. This protein may function in vesicle trafficking, membrane fusion, protein complex assembly and cell motility. Two transcript variants encoding distinct isoforms have been identified.
Supplier:
Matrix Scientific
Description:
MF=C20H13N3O2 MW=327.35 CAS=119139-23-0 MDL=MFCD00236432 1G
Catalog Number:
(100505-026)
Supplier:
Electron Microscopy Sciences
Description:
For negative staining of bacteria. With Basic Fuchsin, staining bacteria spores. Dorner, Le Lait, 6, 8 (1926). Biochem. Biophys. Acta 69,159 (1963).
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Catalog Number:
(10305-440)
Supplier:
Bioss
Description:
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 remodeling, 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.
Catalog Number:
(10305-434)
Supplier:
Bioss
Description:
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 remodeling, 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.
Supplier:
APOLLO SCIENTIFIC
Description:
4-(2-Aminoethyl)cyclohexanol 95%
Catalog Number:
(97061-808)
Supplier:
VWR
Description:
A stain for differentation of E. coli from S. typhosa. Also used in bacteriological media.Color index: 42040
Catalog Number:
(10752-048)
Supplier:
Prosci
Description:
The matrix metalloproteinase (MMP) family are a family of proteins that are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, 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. MMP9 degrades type IV and V collagens and studies suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow and plays a role in tumor-associated tissue remodeling.
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