Datasheet

Biological Description

Specificity	KRIT1 Rabbit mAb recognizes endogenous levels of total KRIT1 protein.
Background	KRIT1 (Krev interaction trapped 1), also known as CCM1, is a scaffolding protein crucial for endothelial cell function, particularly in maintaining blood-brain barrier integrity and regulating vascular morphogenesis. KRIT1 features an N-terminal Nudix domain, three NPxY/F motifs, four ankyrin repeats (forming an ankyrin repeat domain or ARD), and a C-terminal FERM domain subdivided into F1, F2, and F3 lobes. These structural elements mediate interactions with key partners such as Rap1, ICAP1, VE-cadherin, CCM2, and HEG1, all of which play a role in stabilizing endothelial cell junctions, regulating actin cytoskeleton dynamics, and maintaining endothelial barrier function by suppressing RhoA-GTPase activity and preventing excessive actin stress fiber formation. KRIT1 is also central to redox homeostasis, controlling reactive oxygen species (ROS) levels, activating antioxidant defenses, and regulating inflammatory responses. Mutations causing loss of KRIT1 function lead to cerebral cavernous malformation (CCM), a vascular disease marked by abnormal blood vessel formation, endothelial hyperproliferation, and compromised barrier integrity. Additionally, KRIT1 influences various signaling pathways, including PI3K/Akt, mTOR, NF-κB, and NRF2, which regulate cell survival, autophagy, and oxidative stress responses.

Specificity

KRIT1 Rabbit mAb recognizes endogenous levels of total KRIT1 protein.

Background

KRIT1 (Krev interaction trapped 1), also known as CCM1, is a scaffolding protein crucial for endothelial cell function, particularly in maintaining blood-brain barrier integrity and regulating vascular morphogenesis. KRIT1 features an N-terminal Nudix domain, three NPxY/F motifs, four ankyrin repeats (forming an ankyrin repeat domain or ARD), and a C-terminal FERM domain subdivided into F1, F2, and F3 lobes. These structural elements mediate interactions with key partners such as Rap1, ICAP1, VE-cadherin, CCM2, and HEG1, all of which play a role in stabilizing endothelial cell junctions, regulating actin cytoskeleton dynamics, and maintaining endothelial barrier function by suppressing RhoA-GTPase activity and preventing excessive actin stress fiber formation. KRIT1 is also central to redox homeostasis, controlling reactive oxygen species (ROS) levels, activating antioxidant defenses, and regulating inflammatory responses. Mutations causing loss of KRIT1 function lead to cerebral cavernous malformation (CCM), a vascular disease marked by abnormal blood vessel formation, endothelial hyperproliferation, and compromised barrier integrity. Additionally, KRIT1 influences various signaling pathways, including PI3K/Akt, mTOR, NF-κB, and NRF2, which regulate cell survival, autophagy, and oxidative stress responses.

Usage Information

Application

WB, IF

Dilution

WB	IF
1:1000	1:100

Reactivity

Human, Mouse

Source

Rabbit

MW

84 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN₃

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

KRIT1 Rabbit mAb

Biological Description

Usage Information

References

Application Data