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Human MMP9 / Gelatinase B Native Protein LS-G37894

Ordering

Wt. Vol. Conc. Price
5 µg - - $365
Inquire for larger quantities
LSBio (Direct) LSBio (Direct)
206-374-1102
866-206-6909
Orders@LSBio.com
 

Most Popular MMP9 / Gelatinase B Proteins

Human MMP9 / Gelatinase B Recombinant Protein - LS-G5540
E. coli Expression System
None
Unpurified / Endotoxin Level: Less than 0.1 ng/µg of protein.
Human MMP9 / Gelatinase B Recombinant (His) Protein - LS-G17657
E. coli Expression System
His
Unpurified / Lyophilized
Human MMP9 / Gelatinase B Recombinant (His) Protein - LS-G17658
E. coli Expression System
His
Unpurified / Lyophilized

100% Guaranteed 100% Guaranteed
LS-G37894
Native Protein
MMP9 / Gelatinase B
Human
92 kDa, 84 kDa
None
Greater than 95% by SDS-PAGE
350-450 mU/mg after trypsin activation. 1 U is defined as the the amount needed to hydrolyze 1 mol of the peptide, McaProLeuGlyLeuDpaAlaArg per minute.
Tris buffered saline
Store vial at -20°C prior to opening. Centrifuge product if not completely clear after standing at room temperature. Dilute only prior to immediate use. For extended storage aliquot contents and freeze at -20°C or below.
For research use only.

About MMP9 / Gelatinase B

P14780 NM_004994 NP_004985.2

MMP9 Protein, 92kd gelatinase Protein, 92 kd type iv collagenase Protein, 92 kDa gelatinase Protein, 92 kDa type IV collagenase Protein, Matrix metalloproteinase-9 Protein, MMP-9 Protein, Type V collagenase Protein, CLG4B Protein, Gelatinase B Protein, GELB Protein, Macrophage gelatinase Protein, MANDP2 Protein

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. The enzyme encoded by this gene degrades type IV and V collagens.

Requested From: United States
Date Requested: 12/8/2016

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