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Key Documents

SAB4500823

Sigma-Aldrich

Anti-PAR1 (Cleaved-Ser42), N-Terminal antibody produced in rabbit

affinity isolated antibody

Synonym(s):

CXCR-7, CXCR7, G-protein coupled receptor 159, G-protein coupled receptor RDC1, chemokine orphan receptor 1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 46 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

ELISA: 1:20000
western blot: 1:500-1:1000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

proteolytically cleaved (Ser42)

Gene Information

human ... F2R(2149)

General description

Anti-PAR1 (Cleaved-Ser42) Antibody detects endogenous levels of fragment of activated PAR1 (Cleaved-Ser42) protein.
Protease-activated receptor-1 (PAR1), also known as coagulation factor II thrombin receptor (F2R), is encoded by the gene mapped to human chromosome 5q13.3. The encoded protein is a cell surface seven-transmembrane G protein coupled receptor.

Immunogen

The antiserum was produced against synthesized peptide derived from human PAR1.

Immunogen Range: 23-72

Application

Anti-PAR1 (Cleaved-Ser42), N-Terminal antibody produced in rabbit has been used in Western blotting.

Biochem/physiol Actions

Protease-activated receptor-1 (PAR1) facilitates angiogenesis and influences the process of tumor growth and disease progression. In addition, it also plays a vital role in inflammation and thrombosis. Mutation in the gene is associated with an increased risk of metastasis and poorer prognosis of renal cell carcinoma. Elevated expression of the gene has been observed in various types of cancers, such as ovarian, breast, lung, prostate cancer and melanoma.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Zhuang-Zhuang Tang et al.
Naunyn-Schmiedeberg's archives of pharmacology (2021-11-19)
Upregulation of thrombin receptor protease-activated receptor 1 (PAR-1) is verified to contribute to chronic kidney diseases, including diabetic nephropathy; however, the mechanisms are still unclear. In this study, we investigated the effect of PAR-1 on high glucose-induced proliferation of human
Barry S Shea et al.
JCI insight, 2(9) (2017-05-05)
Fibrotic lung disease, most notably idiopathic pulmonary fibrosis (IPF), is thought to result from aberrant wound-healing responses to repetitive lung injury. Increased vascular permeability is a cardinal response to tissue injury, but whether it is mechanistically linked to lung fibrosis
Uncoupling of the profibrotic and hemostatic effects of thrombin in lung fibrosis.
Shea B S, et al.
JCI insight, 2(9) (2017)
Potential importance of protease activated receptor (PAR)-1 expression in the tumor stroma of non-small-cell lung cancer.
Lin C, et al.
BMC Cancer, 17(1), 113-113 (2017)
A novel protease-activated receptor-1 interactor, Bicaudal D1, regulates G protein signaling and internalization.
Swift S, et al.
The Journal of Biological Chemistry, 285(15), 11402-11410 (2010)

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