C1 Esterase Inhibitor Protein

Purified human C1-esterase protein


Product Specifications

Citations3
Description

Purified human C1-esterase protein

Storage

Store at -70°C or below. Avoid freeze/thaw.

Form

Frozen liquid. 10 mM sodium phosphate, 145 mM NaCl, pH 7.3. No preservative, 0.22 µm filtered.

Concentration

1.0 mg/mL (refer to CoA for lot specific concentration)

Applications

See citations and technical data sheet for application info.

Ordering Information

For Research Use Only. Not for use in diagnostic procedures.
Catalog NumberA426
Catalog Number (CE)N/A
Size1.0 ml
Price (USD)$300.00
Price (EURO)240,00 €

Contact us

US Phone+1 (858) 552 1100
EU Phone+353 (91) 412 474
US Emailcontact-us@quidelortho.com
EU Emailcontact-emea@quidelortho.com

Specifications

Description

Purified human C1-esterase protein

Size1.0 ml
Storage

Store at -70°C or below. Avoid freeze/thaw.

Form

Frozen liquid. 10 mM sodium phosphate, 145 mM NaCl, pH 7.3. No preservative, 0.22 µm filtered.

Concentration1.0 mg/mL (refer to CoA for lot specific concentration)
ApplicationsSee citations and technical data sheet for application info.
Purity >95 % by SDS PAGE
SourceNormal human serum
Activity>90 % active protein
Molecular Weight110,000 Da (single chain)
Background

The protease inhibitor C1-INH prevents the spontaneous activation of complement and limits consumption of C2 and C4 by rapidly inactivating C1r, C1s and MASP2. It is the only plasma serine protease inhibitor (Serpin) capable of interacting with and inhibiting activated C1. C1-INH interacts with the catalytic sites of both C1r and C1s. The interaction with activated C1r and C1s is covalent resulting in complexes which are stable to SDS. The binding of C1-INH to activated C1 releases both C1r and C1s from the complex leaving C1q bound to the immune complex. The released complexes contain four molecules: C1-INH-C1r-C1s-C1-INH. The reaction of C1 esterase inhibitor with activated C1 is very fast with the estimated half-life of C1r and C1s being approximately 15 seconds in serum.

Citations

TitleYearApplicationsSample SpeciesSampleSample Details

Venom from Bothrops lanceolatus, a Snake Species Native to Martinique, Potently Activates the Complement System

2018Silver StainHuman

Purified protein

B. lanceolatus venom incubated

Inhibition of aberrant complement activation by a dimer of acetylsalicylic acid.

2015WBHuman

Serum

Acetyl salicylic acid dimer 5,5'-methylenebis(2-acetoxybenzoic acid) (DAS)

P-I snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade.

2013Sliver StainSnake

Bothrops pirajai venom

N/A