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AB47731

Anti-SERPINB1/PI2 antibody

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(6 Publications)

Rabbit Polyclonal SERPINB1/PI2 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Synthetic Peptide within Human SERPINB1.

View Alternative Names

ELANH2, MNEI, PI2, SERPINB1, Leukocyte elastase inhibitor, LEI, Monocyte/neutrophil elastase inhibitor, Peptidase inhibitor 2, Serpin B1, EI, M/NEI, PI-2

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SERPINB1/PI2 antibody (AB47731)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SERPINB1/PI2 antibody (AB47731)

ab47731 (2µg/ml) staining Serpin B1 in human spleen using an automated system (DAKO Autostainer Plus). Using this protocol there is cytoplasmic staining in both red and white pulp.
Sections were rehydrated and antigen retrieved with the Dako 3 in 1 AR buffer citrate pH 6.0 in a DAKO PT link. Slides were peroxidase blocked in 3% H2O2 in methanol for 10 mins. They were then blocked with Dako Protein block for 10 minutes (containing casein 0.25% in PBS) then incubated with primary antibody for 20 min and detected with Dako Envision Flex amplification kit for 30 minutes. Colorimetric detection was completed with Diaminobenzidine for 5 minutes. Slides were counterstained with Haematoxylin and coverslipped under DePeX. Please note that, for manual staining, optimization of primary antibody concentration and incubation time is recommended. Signal amplification may be required.

Western blot - Anti-SERPINB1/PI2 antibody (AB47731)
  • WB

Unknown

Western blot - Anti-SERPINB1/PI2 antibody (AB47731)

All lanes:

Western blot - Anti-SERPINB1/PI2 antibody (ab47731) at 1/1000 dilution

All lanes:

MH-S cell lysate at 20 µL

Predicted band size: 43 kDa

Observed band size: 47 kDa,65 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human SERPINB1. The exact immunogen used to generate this antibody is proprietary information.

P30740

Specificity

This antibody is specific for SERPINB1/PI2.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
Preservative: 0.05% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

SERPINB1 also known as PI2 functions as a serine protease inhibitor. It has an approximate mass of 42 kDa. Serine protease inhibitors play a role in regulating a variety of proteases to maintain cellular homeostasis. This protein mainly expresses in neutrophils epithelial cells and certain immune cells. By inhibiting neutrophil elastase and cathepsin G SERPINB1 protects tissues from protease-driven damage during inflammatory responses.
Biological function summary

SERPINB1 acts to control proteolytic activity and ensures regulated inflammatory responses. It does not form any known complexes but interacts directly with other proteases to modulate their activity. By neutralizing serine proteases SERPINB1 helps in maintaining the balance in immune cell functions. This regulation contributes to the prevention of excessive tissue damage during inflammation emphasizing its role in immune homeostasis.

Pathways

SERPINB1 participates in key regulatory processes such as immune response and protease inhibition pathways. It has a significant influence on pathways involving serine proteases like neutrophil elastase pathways. By interacting with these proteases SERPINB1 modulates their activities ensuring controlled inflammatory reactions and protection against tissue damage.

SERPINB1 links to conditions like chronic obstructive pulmonary disease (COPD) and acute lung injury. These conditions often involve excessive proteolytic activity and SERPINB1 acts to counterbalance this to protect the lung tissue. Additionally the protein shows interactions with other proteins like alpha-1-antitrypsin which also acts as a serine protease inhibitor. The relationship between these proteins highlights their collective role in managing protease activity associated with lung diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis (PubMed : 30692621). Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes but when released from granules, these potent enzymes also destroy host proteins and contribute to mortality. Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3 (PubMed : 11747453, PubMed : 30692621). Also acts as a potent intracellular inhibitor of GZMH by directly blocking its proteolytic activity (PubMed : 23269243). During inflammation, limits the activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation (PubMed : 30692621). When secreted, promotes the proliferation of beta-cells via its protease inhibitory function (PubMed : 26701651).
See full target information SERPINB1

Publications (6)

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

Research (Washington, D.C.) 8:0671 PubMed40230612

2025

Proteogenomic Characterization of High-Grade Lung Neuroendocrine Carcinoma Deciphers Molecular Diversity and Potential Biomarkers of Different Histological Subtypes in Chinese Population.

Applications

Unspecified application

Species

Unspecified reactive species

Zicheng Zhang,Xi Wu,Siqi Bao,Xujie Sun,Fan Yang,Yibo Zhang,Zijian Yang,Liujin Zhang,Ruanqi Chen,Puyuan Xing,Junling Li,Meng Zhou,Lin Yang

Cancer immunology, immunotherapy : CII 65:575-85 PubMed26993499

2016

Oropharyngeal squamous cell carcinomas differentially express granzyme inhibitors.

Applications

Unspecified application

Species

Unspecified reactive species

Pauline M W van Kempen,Rob Noorlag,Justin E Swartz,Niels Bovenschen,Weibel W Braunius,Jeroen F Vermeulen,Ellen M Van Cann,Wilko Grolman,Stefan M Willems

Biotechnology and bioengineering 113:1902-12 PubMed26913574

2016

Proteomic differences in recombinant CHO cells producing two similar antibody fragments.

Applications

WB

Species

Unspecified reactive species

Wolfgang Sommeregger,Patrick Mayrhofer,Willibald Steinfellner,David Reinhart,Michael Henry,Martin Clynes,Paula Meleady,Renate Kunert

PloS one 11:e0151465 PubMed26963506

2016

Pediatric Primitive Neuroectodermal Tumors of the Central Nervous System Differentially Express Granzyme Inhibitors.

Applications

Unspecified application

Species

Unspecified reactive species

Jeroen F Vermeulen,Wim van Hecke,Wim G M Spliet,José Villacorta Hidalgo,Paul Fisch,Roel Broekhuizen,Niels Bovenschen

American journal of physiology. Gastrointestinal a 302:G1163-70 PubMed22421620

2012

Serpin B1 protects colonic epithelial cell via blockage of neutrophil elastase activity and its expression is enhanced in patients with ulcerative colitis.

Applications

IHC-P, WB

Species

Human, Human

Kazuhiko Uchiyama,Yuji Naito,Tomohisa Takagi,Katsura Mizushima,Yasuko Hirai,Natsuko Hayashi,Akihito Harusato,Ken Inoue,Kohei Fukumoto,Shinya Yamada,Osamu Handa,Takeshi Ishikawa,Nobuaki Yagi,Satoshi Kokura,Toshikazu Yoshikawa

Oral oncology 45:771-6 PubMed19213596

2009

Serine protease inhibitor (SERPIN) B1 promotes oral cancer cell motility and is over-expressed in invasive oral squamous cell carcinoma.

Applications

IHC-P, WB

Species

Human, Human

Mei-Yu Tseng,Shyun-Yeu Liu,Hau-Ren Chen,Yu-Jen Wu,Chien-Chih Chiu,Po-Ting Chan,Wei-Fan Chiang,Yu-Chi Liu,Chien-Yu Lu,Yuh-Shan Jou,Jeff Yi-Fu Chen
View all publications

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