Synthetic peptide directed towards the middle region of human HABP2
Biochem/physiol Actions
HABP2 is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. It is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. The protein encoded by this gene is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. The encoded protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Sequence
Synthetic peptide located within the following region: EPSTKLPGFDSCGKTEIAERKIKRIYGGFKSTAGKHPWQASLQSSLPLTI
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.