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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Integrins are transmembrane proteins that are involved in interactions cell-to-cell and cell-to-extracellular matrix (ECM) adhesion. Integrins play diverse roles including cell migration, development, wound healing, differentiation, and apoptosis. Integrin alpha 10 subunit (ITGA10), along with integrin beta 1, is thought to be an essential part of a novel collagen type II receptor expressed mainly in chondrocytes and cartilage tissue.
References
Product Information
Format
Affinity Purified
Control
SW-1353 cell lysate
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Detect Integrin alpha 10 (ITGA10) using this Anti-Integrin alpha 10 (ITGA10) Antibody validated for use in WB.
Key Applications
Western Blotting
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to the extracellular domain of human Integrin alpha-10.
Epitope
Extracellular Domain
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
This antibody recognizes the extracellular domain of Integrin alpha 10.
Species Reactivity
Human
Pig
Rhesus Macaque
Chimpanzee
Canine
Primate
Species Reactivity Note
Demonstrated to react with human. Predicted to react with pig, rhesus monkey, chimpanzee, and canine based on 100% sequence homology. Other homologies: rat (93% sequence homology).
Summary: Integrins are integral membrane proteins composed of an alpha chain and a beta chain, and are known to participate in cell adhesion as well as cell-surface mediated signalling. The I-domain containing alpha 10 combines with the integrin beta 1 chain (ITGB1) to form a novel collagen type II-binding integrin expressed in cartilage tissue. [provided by RefSeq].
FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.
SUBUNIT STRUCTURE: Heterodimer of an alpha and a beta subunit. Alpha-10 associates with beta-1.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Widely expressed with highest expression in muscle and heart. Found in articular cartilage.
DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.
SEQUENCE SIMILARITIES: Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats. Contains 1 VWFA domain.
Molecular Weight
~127 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in SW-1353 cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected integrin alpha10 in 10 µg of SW-1353 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Expression of integrin alpha 10 is transcriptionally activated by pRb in mouse osteoblasts and is downregulated in multiple solid tumors. Engel, BE; Welsh, E; Emmons, MF; Santiago-Cardona, PG; Cress, WD Cell death & disease
4
e938
2013
pRb is known as a classic cell cycle regulator whose inactivation is an important initiator of tumorigenesis. However, more recently, it has also been linked to tumor progression. This study defines a role for pRb as a suppressor of the progression to metastasis by upregulating integrin α10. Transcription of this integrin subunit is herein found to be pRb dependent in mouse osteoblasts. Classic pRb partners in cell cycle control, E2F1 and E2F3, do not repress transcription of integrin α10 and phosphorylation of pRb is not necessary for activation of the integrin α10 promoter. Promoter deletion revealed a pRb-responsive region between -108 bp to -55 bp upstream of the start of the site of transcription. pRb activation of transcription also leads to increased levels of integrin α10 protein and a greater concentration of the integrin α10 protein at the cell membrane of mouse osteoblasts. These higher levels of integrin α10 correspond to increased binding to collagen substrate. Consistent with our findings in mouse osteoblasts, we found that integrin α10 is significantly underexpressed in multiple solid tumors that have frequent inactivation of the pRb pathway. Bioinformatically, we identified data consistent with an 'integrin switch' that occurs in multiple solid tumors consisting of underexpression of integrins α7, α8, and α10 with concurrent overexpression of integrin β4. pRb promotes cell adhesion by inducing expression of integrins necessary for cell adhesion to a substrate. We propose that pRb loss in solid tumors exacerbates aggressiveness by debilitating cellular adhesion, which in turn facilitates tumor cell detachment and metastasis.
