Measured by its binding ability in a functional ELISA. When Collagen I is immobilized at 5 μg/mL, Recombinant Mouse Integrin alpha 1 beta 1 can bind with an apparent Kd <5 nM. Optimal dilutions should be determined by each laboratory for each application.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Integrin alpha 1 beta 1 protein
Phe29 (Integrin alpha 1) & No results obtained: Gln21 predicted (Integrin beta 1), sequencing might be blocked
Structure / Form
Noncovalently-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE with silver staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
132 kDa (Integrin alpha 1) & 86.5 kDa (Integrin beta 1). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
120-135 kDa & 180-215 kDa, reducing conditions
Publications
Read Publications using 8188-AB in the following applications:
Integrin alpha 1 beta 1, also called VLA1, is the only alpha 1 integrin family adhesion receptor, one of twelve integrins that share the beta 1 subunit, and one of four collagen-binding integrins (1-6). It is the non-covalent heterodimer of 190-210 kDa alpha 1 (CD49a) and 130 kDa beta 1 (CD29) type I transmembrane glycoprotein subunits. It is found on cells including activated T cells, B cells, monocytes, vascular smooth muscle cells, osteoblasts and adipocytes (2, 7-9). The alpha 1 extracellular domain (ECD) contains an I (inserted) domain which includes the ligand binding site (2, 4). The beta 1 ECD contains a vWFA domain, which participates in binding (3). Each subunit then has a transmembrane sequence and a short cytoplasmic tail. Divalent cations and intracellular (inside-out) signaling convert the dimer from the folded, inactive form to its most active, extended conformation (1, 2). The 1113 amino acid (aa) mouse alpha 1 extracellular domain (ECD) shares 88% and 96% aa sequence identity with human and rat alpha 1, respectively, while the 708 aa mouse beta 1 ECD shares 93% and 98% aa sequence identity with human and rat beta 1, respectively. alpha 1 beta 1 preferentially binds collagens I, IV, VI, XIII and XVI, but also binds laminin (4-11). alpha 1 beta 1 is reported to down-regulate EGF R signaling, increase expression of caveolin-1, reduce production of reactive oxygen species, regulate collagen expression, control MMP collagenase and gelatinase activity, and mediate the renal basement membrane disorder Alport syndrome (11-13). These effects may begin by alpha 1 beta 1 binding of caveolin-1, initiating signaling pathways that involve the phosphatase TC-PTP, kinases ERK and p38, and the transcription factor PPAR-gamma (11-14). alpha 1 beta 1 down-regulates MMP-mediated angiostatin formation, enhancing tumor vascularization (9). alpha 1 beta 1-null mice are deficient in fibroblast collagen IV and laminin-mediated cell spreading and migration, show defects in bone healing, and are resistant to Alport renal fibrosis (10-12, 15). When expressed in the same epithelial cells, alpha 1 beta 1 negatively regulates integrin alpha 2 beta 1-mediated cell adhesion and migration (16).
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