The serine proteinase inhibitors (serpins) compose a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. The monocyte/neutrophil elastase inhibitor gene, SERPINB1, belongs to the Ov-serpin family (ovalbumin-related serpins). Human SerpinB1, also designated monocyte/neutrophil elastase inhibitor (M/NEI) or leukocyte elastase inhibitor (LEI), is a cytoplasmic protein which acts as a fast-acting stoichiometric proteinase inhibitor that regulates the activity of neutrophil elastase (NE), cathepsin-G and proteinase-3. There are four homologous genes in mouse designated SerpinB1a, SerpinB1b, SerpinB1c and the pseudogene, Serpinb1-ps1. The three protein-coding genes share significant sequence identity, however SerpinB1a (also designated EIA) has been characterized as the functional ortholog of human SerpinB1.

Anti elastase; EI; ELANH2; ILEU_HUMAN; LEI; Leukocyte elastase inhibitor; M/NEI; MNEI; Monocyte/neutrophil elastase inhibitor; Peptidase inhibitor 2; Pi-2; PI2; Serine (or cysteine) proteinase inhibitor clade B (ovalbumin) member 1; Serpin B1; Serpin peptidase inhibitor clade B (ovalbumin) member 1; serpinb1.

Human,Mouse,Rat

WB

WB 1:500-2000

43kD

1992

P30740

https://www.uniprot.org/uniprotkb/P30740

Cytoplasm.

KLH conjugated synthetic peptide derived from human SERPINB1

Rabbit

Polyclonal

IgG

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.