Datasheet

Biological Description

Specificity	Anti-Integrin α 5 Rabbit Antibody [K23D13] detects endogenous levels of total Integrin α 5 protein.
Background	Integrin α5 is a type I transmembrane glycoprotein that pairs with β1 to form the α5β1 heterodimeric receptor, primarily recognizing fibronectin, a major extracellular matrix (ECM) component. The α5 subunit contains an N-terminal seven-bladed beta-propeller domain responsible for ligand binding, and a cytoplasmic tail that interacts with intracellular signaling and cytoskeletal proteins, facilitating bidirectional signal transduction. Integrin α5β1 plays a pivotal role in cell adhesion, migration, and ECM organization, thereby influencing processes such as embryonic development, tissue repair, angiogenesis, and tumor progression. Its ligand-binding affinity and activation state are regulated by conformational changes driven by divalent cations (e.g., Mn2+, Mg2+) and interactions with the synergy site on fibronectin. Integrin α5β1 activation promotes focal adhesion assembly, linking the ECM to the actin cytoskeleton and triggering signaling cascades that regulate cell shape, proliferation, and survival via pathways like FAK, Src, and MAPK. Regulation of α5 integrin is finely tuned through inside-out signaling via talin and kindlin binding to its cytoplasmic tail, altering its affinity for fibronectin. Additionally, the interaction with urokinase plasminogen activator receptor (uPAR) modulates its conformation and function, influencing adhesion and migration dynamics. Dysregulation of α5β1 integrin is implicated in pathological conditions including cancer metastasis, fibrosis, and vascular diseases.

Specificity

Anti-Integrin α 5 Rabbit Antibody [K23D13] detects endogenous levels of total Integrin α 5 protein.

Background

Integrin α5 is a type I transmembrane glycoprotein that pairs with β1 to form the α5β1 heterodimeric receptor, primarily recognizing fibronectin, a major extracellular matrix (ECM) component. The α5 subunit contains an N-terminal seven-bladed beta-propeller domain responsible for ligand binding, and a cytoplasmic tail that interacts with intracellular signaling and cytoskeletal proteins, facilitating bidirectional signal transduction. Integrin α5β1 plays a pivotal role in cell adhesion, migration, and ECM organization, thereby influencing processes such as embryonic development, tissue repair, angiogenesis, and tumor progression. Its ligand-binding affinity and activation state are regulated by conformational changes driven by divalent cations (e.g., Mn2+, Mg2+) and interactions with the synergy site on fibronectin. Integrin α5β1 activation promotes focal adhesion assembly, linking the ECM to the actin cytoskeleton and triggering signaling cascades that regulate cell shape, proliferation, and survival via pathways like FAK, Src, and MAPK. Regulation of α5 integrin is finely tuned through inside-out signaling via talin and kindlin binding to its cytoplasmic tail, altering its affinity for fibronectin. Additionally, the interaction with urokinase plasminogen activator receptor (uPAR) modulates its conformation and function, influencing adhesion and migration dynamics. Dysregulation of α5β1 integrin is implicated in pathological conditions including cancer metastasis, fibrosis, and vascular diseases.

Usage Information

Application

WB, IP, IHC, IF , FCM

Dilution

WB	IP	IHC	IF	FCM
1:1000 - 1:10000	1:10 - 1:100	1:400	1:50	1:20

Reactivity

Mouse, Rat, Human

Source

Rabbit

MW

115 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

References

https://pubmed.ncbi.nlm.nih.gov/15684035/
https://pubmed.ncbi.nlm.nih.gov/33962943/

Anti-Integrin α 5 Rabbit Antibody [K23D13]

Biological Description

Usage Information

References

Application Data