Kar2, also known as BiP (Immunoglobulin heavy-chain-binding protein), is a vital chaperone protein localized in the endoplasmic reticulum (ER) of eukaryotic cells. Its primary function revolves around the regulation of protein folding and assembly within the ER, playing a crucial role in protein quality control and ER homeostasis. Kar2/BiP interacts with nascent polypeptides as they enter the ER, assisting in their folding into functional three-dimensional structures and preventing the aggregation of misfolded or unfolded proteins. Moreover, Kar2/BiP functions as a key regulator of the unfolded protein response (UPR), a cellular stress response pathway activated upon ER stress to restore ER function and alleviate protein misfolding. Through its interaction with transmembrane sensor proteins such as Ire1, Perk, and ATF6, Kar2/BiP orchestrates the UPR signaling cascade, modulating gene expression and promoting adaptive responses to ER stress.
Activation of Kar2/BiP is intricately regulated to ensure its optimal function in protein folding and ER stress response pathways. One of the primary mechanisms of activation involves the binding of nucleotides, particularly ATP and ADP, to the nucleotide-binding domain of Kar2/BiP. ATP binding induces a conformational change in Kar2/BiP, promoting its association with unfolded or misfolded proteins and facilitating their folding. Conversely, the hydrolysis of ATP to ADP triggers another conformational change in Kar2/BiP, leading to the release of folded proteins and the dissociation of Kar2/BiP from its client proteins. Additionally, post-translational modifications such as phosphorylation can modulate Kar2/BiP activity, influencing its interaction with client proteins and its participation in UPR signaling pathways. Collectively, the precise regulation of Kar2/BiP activation ensures efficient protein folding and ER stress response, safeguarding cellular homeostasis under physiological and stress conditions.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin induces ER stress by inhibiting the ER calcium ATPase, leading to calcium depletion from the ER and activation of the UPR, potentially increasing Kar2 expression. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, resulting in protein misfolding in the ER and activation of the UPR, which could upregulate Kar2 expression. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $31.00 $53.00 $124.00 $374.00 | 25 | |
Brefeldin A disrupts protein trafficking from the ER to the Golgi apparatus, potentially leading to ER stress and increased Kar2 expression. | ||||||
Homocysteine | 6027-13-0 | sc-507315 | 250 mg | $195.00 | ||
Elevated homocysteine levels have been associated with ER stress, which might result in upregulation of Kar2 as a response. | ||||||
Valproic Acid | 99-66-1 | sc-213144 | 10 g | $87.00 | 9 | |
Valproic acid can induce ER stress, potentially leading to the increased expression of Kar2. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin interferes with the function of Hsp90, potentially leading to protein misfolding and increased Kar2 expression. | ||||||
Betulinic Acid | 472-15-1 | sc-200132 sc-200132A | 25 mg 100 mg | $117.00 $344.00 | 3 | |
Betulinic Acid can induce ER stress, potentially leading to upregulated Kar2 expression. | ||||||