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K1632

Sigma-Aldrich

Kininogen high molecular weight, Two Chain from human plasma

lyophilized powder

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About This Item

MDL number:
MFCD00131428
UNSPSC Code:
12352202
NACRES:
NA.61

RM 364.00

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biological source

human plasma

Quality Level

200

form

lyophilized powder

solubility

H2O: soluble 0.1 mg protein/mL

UniProt accession no.

P01042

storage temp.

−20°C

Gene Information

human ... KNG1(3827), KNG1 (includes EG:3827)

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This Item
H9291F4883B1901
Kininogen high molecular weight, Two Chain from human plasma lyophilized powder

K1632

Kininogen high molecular weight, Two Chain from human plasma

Hemopexin from human plasma ≥95% (SDS-PAGE), lyophilized powder

H9291

Hemopexin from human plasma

Fibrinogen from human plasma 35-65% protein (≥90% of protein is clottable).

F4883

Fibrinogen from human plasma

Bradykinin Fragment 2-9 ≥97% (HPLC)

B1901

Bradykinin Fragment 2-9

biological source

human plasma

biological source

human plasma

biological source

human plasma

biological source

-

form

lyophilized powder

form

lyophilized powder

form

powder

form

powder

solubility

H2O: soluble 0.1 mg protein/mL

solubility

-

solubility

0.9% NaCl: soluble

solubility

-

Gene Information

human ... KNG1(3827), KNG1 (includes EG:3827)(3827)

Gene Information

human ... HPX(3263)

Gene Information

human ... FGA(2243), FGB(2244), FGG(2266)

Gene Information

human ... KNG1 (includes EG:3827)(3827)

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

UniProt accession no.

P01042

UniProt accession no.

-

UniProt accession no.

P02671, P02675, P02679

UniProt accession no.

P01042

General description

HK (KNG1) gene is mapped to human chromosome 3q27.3. It is a glycoprotein.[1]
High-molecular-weight kininogen (HK) is the substrate and cofactor of the plasma kallikrein-kinin system (KKS). It is present at a concentration of 660 nM on the plasma and binds to platelet GPI-V-IX complex.

Biochem/physiol Actions

High molecular weight kininogen, two chain, is a participant in contact phase activation of the intrinsic blood coagulation cascade that forms a substrate on which blood factor XI is held in proximity to factor XII allowing reciprocal activation of the two factors. It is also involved in the activation of prekallikrein. High molecular weight kininogen binds to proteoglycans on the surface of platelets, endothelial cells, and other cell types. Domain 5 of high molecular weight kininogen inhibits platelet aggregation and angiogenesis.
High-molecular-weight kininogen (HK) inhibits binding of thrombin to platelets.[2]

Packaging

Package size based on protein content

Physical form

Lyophilized from 4 mM sodium acetate, pH 5.3, 0.15 M NaCl

Preparation Note

Prepared by kallikrein digestion of human kininogen. Purified to remove kallikrein and kinin.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves
  • Specification Sheet

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    Certificates of Analysis (COA)

    Lot/Batch Number
    SLCJ4159
    SLCG0116
    SLCD1357
    SLBX5903
    SLBT1691

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    Henri Weidmann et al.
    Biochimica et biophysica acta. Molecular cell research, 1864(11 Pt B), 2118-2127 (2017-07-27)
    The contact system is a potent procoagulant and proinflammatory plasma protease cascade that is initiated by binding ("contact")-induced, auto-activation of factor XII zymogen. Formed active serine protease FXIIa then cleaves plasma prekallikrein to kallikrein that in turn liberates the mediator
    [Omeprazole long-term therapy: how great is the risk of developing a carcinoid tumor?].
    H Koop
    Zeitschrift fur Gastroenterologie, 26(12), 769-771 (1988-12-01)
    Rince John et al.
    FEBS letters, 591(21), 3507-3522 (2017-09-28)
    Cytoglobin (Cygb) is a cellular haemoprotein belonging to the globin family with ambiguous biological functions. Downregulation of Cygb in many cancers is indicative of its tumour-suppressive role. This is the first report showing the cell cycle regulation of Cygb, which

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