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Mouse Anti-KNG1 Recombinant Antibody (15G5-A11) (CBMAB-K1443-LY)

This product is antibody recognizes KNG1. The antibody 15G5-A11 immunoassay techniques such as: EIA, WB.
See all KNG1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
15G5-A11
Antibody Isotype
IgG2b
Application
EIA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
1 mg/mL
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Kininogen 1
Introduction
This gene uses alternative splicing to generate two different proteins- high molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK). HMWK is essential for blood coagulation and assembly of the kallikrein-kinin system. Also, bradykinin, a peptide causing numerous physiological effects, is released from HMWK. Bradykinin also functions as an antimicrobial peptide with antibacterial and antifungal activity. In contrast to HMWK, LMWK is not involved in blood coagulation. Three transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Nov 2014]
Entrez Gene ID
3827
UniProt ID
P01042
Alternative Names
Kininogen 1; Alpha-2-Thiol Proteinase Inhibitor; Williams-Fitzgerald-Flaujeac Factor; High Molecular Weight Kininogen; Fitzgerald Factor; Bradykinin; HMWK;
Function
(1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.
Biological Process
Antimicrobial humoral immune response mediated by antimicrobial peptideIDA:UniProtKB
Blood coagulationIEA:UniProtKB-KW
Inflammatory responseIEA:UniProtKB-KW
Killing of cells of other organismIDA:UniProtKB
Negative regulation of blood coagulationManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of cell adhesionManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of endopeptidase activityManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of proteolysisManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of apoptotic process1 PublicationNAS:UniProtKB
Positive regulation of cytosolic calcium ion concentrationManual Assertion Based On ExperimentIDA:UniProtKB
VasodilationIEA:UniProtKB-KW
Cellular Location
Secreted, extracellular space
Involvement in disease
High molecular weight kininogen deficiency (HMWK deficiency):
Autosomal recessive coagulation defect. Patients with HWMK deficiency do not have a hemorrhagic tendency, but they exhibit abnormal surface-mediated activation of fibrinolysis.
PTM
Bradykinin is released from kininogen by plasma kallikrein.
Hydroxylation of Pro-383 oCcurs prior to the release of bradykinin.
Phosphorylated by FAM20C in the extracellular medium.
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.

Adenaeuer, A., Barco, S., Trinchero, A., Krutmann, S., Nazir, H. F., Ambaglio, C., ... & Rossmann, H. (2023). Severe high-molecular-weight kininogen deficiency: clinical characteristics, deficiency–causing KNG1 variants, and estimated prevalence. Journal of thrombosis and haemostasis, 21(2), 237-254.

Cheng, X., Liu, D., Song, H., Tian, X., Yan, C., & Han, Y. (2021). Overexpression of Kininogen-1 aggravates oxidative stress and mitochondrial dysfunction in DOX-induced cardiotoxicity. Biochemical and biophysical research communications, 550, 142-150.

Vijay, A., Kassab, M. B., Shim, Y. J., Swaidani, S., Mauskapf, A., McCrae, K. R., & Jaffer, F. A. (2021). Protective Effects of Kininogen-1 Gene Deficiency in Mouse Models of Venous Thrombosis. Blood, 138, 289.

Adenaeuer, A., Barco, S., Trinchero, A., Nazir, H., Krutmann, S., Ambaglio, C., ... & Lämmle, B. (2021). Severe High Molecular Weight Kininogen (HK) Deficiency: Clinical Characteristics, Deficiency-Causing KNG1 Variants in Reported and New Cases, and Estimated Prevalence. Blood, 138(Supplement 1), 3200-3200.

Jeong, D., Goo, J. Y., Kim, H. K., Chong, S. Y., & Kang, M. S. (2020). The first korean case of high-molecular-weight kininogen deficiency, with a novel variant, c. 488delG, in the KNG1 gene. Annals of laboratory medicine, 40(3), 264.

Wang, W., Wang, S., & Zhang, M. (2020). Evaluation of kininogen 1, osteopontin and α‑1‑antitrypsin in plasma, bronchoalveolar lavage fluid and urine for lung squamous cell carcinoma diagnosis. Oncology letters, 19(4), 2785-2792.

Yu, J., Huang, Y., Lin, C., Li, X., Fang, X., Zhong, C., ... & Zheng, S. (2018). Identification of kininogen 1 as a serum protein marker of colorectal adenoma in patients with a family history of colorectal cancer. Journal of Cancer, 9(3), 540.

Xu, J., Fang, J., Cheng, Z., Fan, L., Hu, W., Zhou, F., & Shen, H. (2018). Overexpression of the Kininogen-1 inhibits proliferation and induces apoptosis of glioma cells. Journal of Experimental & Clinical Cancer Research, 37, 1-15.

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For research use only. Not intended for any clinical use.

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