![]() Glu-C structure
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Common Name | Glu-C | ||
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CAS Number | 66676-43-5 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | N/A | Melting Point | N/A | |
MSDS | Chinese USA | Flash Point | N/A | |
Symbol |
![]() ![]() GHS07, GHS08 |
Signal Word | Danger |
Name | EC 3.4.21.19 |
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Synonym | More Synonyms |
Appearance of Characters | lyophilized powder |
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Storage condition | −20°C |
Water Solubility | Soluble in water |
Symbol |
![]() ![]() GHS07, GHS08 |
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Signal Word | Danger |
Hazard Statements | H315-H317-H319-H334-H335 |
Precautionary Statements | P261-P280-P305 + P351 + P338-P342 + P311 |
Personal Protective Equipment | dust mask type N95 (US);Eyeshields;Faceshields;Gloves |
Hazard Codes | Xn |
Risk Phrases | 36/37/38-42/43 |
Safety Phrases | 22-24-26-36/37-45 |
RIDADR | NONH for all modes of transport |
WGK Germany | 3 |
pNovo+: de novo peptide sequencing using complementary HCD and ETD tandem mass spectra.
J. Proteome Res. 12(2) , 615-25, (2013) De novo peptide sequencing is the only tool for extracting peptide sequences directly from tandem mass spectrometry (MS) data without any protein database. However, neither the accuracy nor the effici... |
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Probing the 3-D structure, dynamics, and stability of bacterial collagenase collagen binding domain (apo- versus holo-) by limited proteolysis MALDI-TOF MS.
J. Am. Soc. Mass Spectrom. 23(3) , 505-19, (2012) Pairing limited proteolysis and matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) to probe clostridial collagenase collagen binding domain (CBD) reveals the s... |
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Propeptide processing and proteolytic activity of proenzymes of the staphylococcal and enterococcal GluV8-family protease.
Indian J. Biochem. Biophys. 49(6) , 421-7, (2012) Proenzymes with various lengths of propeptides have been observed in GluV8 from Staphylococcus aureus and GluSE from S. epidermidis. However, the production mechanism of these proenzymes and roles of ... |
MFCD01324998 |