HRP Anti-V5 tag抗体[E10/V4RR]

补充信息

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The V5 tag is an epitope tag derived from the P and V fusion proteins of the paramyxovirus. It typically measures around 14 amino acids in length and is often used in molecular biology for tagging and protein expression studies. In terms of mechanical function the V5 tag facilitates the detection characterization and purification of recombinant proteins. Scientists commonly use it in various hosts such as bacteria yeast and mammalian cells due to its convenient integration into larger protein complexes. Unlike native proteins it serves as a non-disruptive label for identifying proteins without affecting their functionality.

Biological function summary

Researchers employ the V5 tag to decipher protein localization expression and role within cellular environments. It allows easy tracking in situ by using antibodies that target the V5 epitope such as the anti-V5 antibody. The V5 tag proves effective in dual-tagging systems useful in elucidating protein interactions and complex formations for instance when combined with other tags like biotin tag or APC tag. This assists in isolating and identifying components of complex cellular machinery.

Pathways

The tag is frequently utilized in studies exploring functional pathways of various proteins across metabolic and signaling pathways. It aids in examining the relationship between proteins within signaling cascades by tagging proteins that interact with others such as those in the PK tag-related signaling pathways. Researchers often track proteins across intricate networks to understand cellular processes intricately using V5-tagged proteins as indicators or reporters.

Scientists harness the V5 tag to investigate the expression and interactions of proteins associated with certain conditions such as cancer and neurodegenerative diseases. Through its integration scientists aim to uncover alterations in protein interactions or localizations that contribute to disease progression. For example they may tag proteins linked to cancer pathways observing how disruptions in proteins related to anti-V5 targets could provide insights into tumor biology or pathogenesis.