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AB280938

Native human Neutrophil Elastase protein (Active)

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(1 Publication)

Native human Neutrophil Elastase protein (Active) is a Human Full Length protein, in the 30 to 267 aa range, expressed in Native, with >95%, suitable for SDS-PAGE, FuncS, ELISA.

View Alternative Names

ELA2, ELANE, Neutrophil elastase, Bone marrow serine protease, Elastase-2, Human leukocyte elastase, Medullasin, PMN elastase, HLE

Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Tags

Tag free

Applications

ELISA, SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

1 unit hydrolyzes one μmole per minute of MeO-Suc-Ala-Ala-Pro-Val-pNA at 25°C, in 100mM Tris-Hcl, pH 7.5 with 500mM NaCl.

Specific activity = ≥20 U/mg protein.

Accession

P08246

Animal free

No

Carrier free

Yes

Species

Human

Storage buffer

pH: 5.5 Constituents: 0.87% Sodium chloride, 0.41% Sodium acetate

storage-buffer

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Primary Antibodies

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

ab280938 was prepared from whole blood shown to be non-reactive for HbsAG, anti-HCV, anti HBc, and negative for HIV 1 & 2 by FDA approved tests.

This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the protein. Should this product contain a precipitate we recommend microcentrifugation before use.

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Sequence info

[{"sequence":"IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH","proteinLength":"Full Length","predictedMolecularWeight":"29 kDa","actualMolecularWeight":null,"aminoAcidEnd":267,"aminoAcidStart":30,"nature":"Native","expressionSystem":"Native","accessionNumber":"P08246","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Neutrophil Elastase also known as neutrophil proteinase 3 has a molecular mass of approximately 30 kDa. It is a serine protease expressed mainly in azurophilic granules of neutrophils. This enzyme breaks down various proteins including elastin at sites of inflammation. Neutrophil Elastase releases during degranulation or through neutrophil extracellular traps (NETs) to combat pathogens.
Biological function summary

The target plays a significant role in neutrophil-mediated tissue remodeling and host defense. It leads to the breaking down of extracellular matrix components contributing to tissue remodeling and repair. Neutrophil Elastase is part of a complex interplay with other proteases like matrix metalloproteinases (MMPs). Its activity is regulated by endogenous inhibitors such as alpha-1 antitrypsin to prevent excessive tissue damage.

Pathways

This protease is important in inflammation and immune response pathways. It plays a role in the complement system by activating C5 a component of the complement cascade. It also acts in conjunction with other proteases such as cathepsin G to modulate immune and inflammatory responses. Neutrophil Elastase's role within these pathways is pivotal for the regulation of inflammation and destruction of pathogens.

Individuals with conditions such as chronic obstructive pulmonary disease (COPD) and cystic fibrosis often exhibit dysregulation or excessive activity of Neutrophil Elastase. This excessive activity leads to tissue damage and exacerbates disease progression. The enzyme also interacts with proteins like elastin and collagen in these diseases further contributing to pathological tissue remodeling and damage.
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Specifications

Form

Liquid

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General info

Function

Serine protease that modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed : 15140022). Promotes cleavage of GSDMB, thereby inhibiting pyroptosis (PubMed : 36899106). Promotes blood coagulation (PubMed : 20676107). Through the activation of the platelet fibrinogen receptor integrin alpha-IIb/beta-3, potentiates platelet aggregation induced by a threshold concentration of cathepsin G (CTSG) (PubMed : 25211214, PubMed : 9111081). Cleaves and thus inactivates tissue factor pathway inhibitor (TFPI) (PubMed : 20676107, PubMed : 25211214). Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae (PubMed : 10947984).

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

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Product protocols

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Target data

Serine protease that modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed : 15140022). Promotes cleavage of GSDMB, thereby inhibiting pyroptosis (PubMed : 36899106). Promotes blood coagulation (PubMed : 20676107). Through the activation of the platelet fibrinogen receptor integrin alpha-IIb/beta-3, potentiates platelet aggregation induced by a threshold concentration of cathepsin G (CTSG) (PubMed : 25211214, PubMed : 9111081). Cleaves and thus inactivates tissue factor pathway inhibitor (TFPI) (PubMed : 20676107, PubMed : 25211214). Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae (PubMed : 10947984).
See full target information ELANE
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Pharmaceuticals (Basel, Switzerland) 15: PubMed35631327

2022

Camostat Does Not Inhibit the Proteolytic Activity of Neutrophil Serine Proteases.

Applications

Unspecified application

Species

Unspecified reactive species

Akmaral Assylbekova,Anuar Zhanapiya,Renata Grzywa,Marcin Sienczyk,Christian Schönbach,Timo Burster
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