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Merck

SAB4200823

Sigma-Aldrich

Anti- Protease-7 antibody produced in rabbit

affinity isolated antibody

Sinónimos:

Omptin, Outer membrane protein 3B, Protease A, Protease VII

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

antibody form

affinity isolated antibody

antibody product type

primary antibodies

description

Research area: Microbiome

form

buffered aqueous solution

species reactivity

E. coli, Shigella flexneri

packaging

antibody small pack of 25 μL

concentration

~1.0 mg/mL

technique(s)

immunoblotting: 0.5-1 μg/mL using E. coli lysate.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

Escherichia coli K12 ... ompT(945185)
Shigella flexneri ... ompT(1238162)

Categorías relacionadas

General description

E. coli Protease-7, also known as Omptin (ompT) or Outer membrane protein 3B, belongs to the omptin family of outer membrane proteases found in several Gram-negative bacteria of the Enterobacteriaceae family. Omptins are unique proteases combining features of both serine and aspartate proteases activity. Several group members may also have cysteine protease and metalloproteases activities, all share a conserved active site. The enzyme proteolytic activity is dependent on the interaction with the lipid A region of the lipopolysaccharide (LPS).

Immunogen

Synthetic peptide corresponding to human N-terminal region E.coli Protease7, conjugated to KLH

Application

Anti-Protease-7 antibody specifically recognizes Protease-7 from E. coli and Shigella flexneri and does not cross react with Proteus mirabilis. The antibody may be used in various immunochemical techniques including Immunoblotting (doublet ~35 kDa).

Physical form

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

Disclaimer

This product is for R&D use only, not for drug, household, or other uses.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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L Vandeputte-Rutten et al.
The EMBO journal, 20(18), 5033-5039 (2001-09-22)
OmpT from Escherichia coli belongs to a family of highly homologous outer membrane proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram-negative bacteria. Here we present the crystal structure of OmpT, which shows a 10-stranded
Akiko Urashima et al.
Cellular microbiology, 19(11) (2017-06-18)
Antimicrobial peptides (AMPs) are important components of the innate immune system. Enterohaemorrhagic Escherichia coli (EHEC), a food-borne pathogen causing serious diarrheal diseases, must overcome attack by AMPs. Here, we show that resistance of EHEC against human cathelicidin LL-37, a primary
Jenny-Lee Thomassin et al.
Infection and immunity, 80(2), 483-492 (2011-12-07)
Enterohemorrhagic Escherichia coli (EHEC) and enteropathogenic E. coli (EPEC) are food-borne pathogens that cause serious diarrheal diseases. To colonize the human intestine, these pathogens must overcome innate immune defenses such as antimicrobial peptides (AMPs). Bacterial pathogens have evolved various mechanisms
John R Brannon et al.
Infection and immunity, 83(6), 2300-2311 (2015-04-01)
Bacterial proteases are important virulence factors that inactivate host defense proteins and contribute to tissue destruction and bacterial dissemination. Outer membrane proteases of the omptin family, exemplified by Escherichia coli OmpT, are found in some Gram-negative bacteria. Omptins cleave a

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