Human Recombinant KNG1 protein, His Tag (V2LY-0526-LY5164)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant KNG1 protein, His Tag consist of Amino Acid: 19-644 and predicts a molecular mass of 71.3 kDa.
Molecule Mass
71.3 kDa
Verified
HPLC
Sequence
Amino Acid: 19-644
Species
Human

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

Purity
≥85% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tirs, NaCl, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Kininogen 1
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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