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SAB4200823

Sigma-Aldrich

Anti- Protease-7 antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Description

Research area: Microbiome

Forme

buffered aqueous solution

Espèces réactives

E. coli, Shigella flexneri

Conditionnement

antibody small pack of 25 μL

Concentration

~1.0 mg/mL

Technique(s)

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

Numéro d'accès UniProt

P09169

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Catégories apparentées

Description générale

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).

Immunogène

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).

Forme physique

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

Clause de non-responsabilité

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

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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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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