Recombinant Mouse Integrin alpha 1 beta 1 Protein, CF
Recombinant Mouse Integrin alpha 1 beta 1 Protein, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
Mouse Integrin alpha 1 (Phe29-Pro1141) Accession # Q3V3R4 |
His-Pro | GGGSGGGS | Acidic Tail | 6-His tag |
Mouse Integrin beta 1 (Gln21-Asp728) Accession # P09055 |
His-Pro | GGGSGGGS | Basic Tail | |
N-terminus | C-terminus | |||
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
8188-AB
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Integrin alpha 1 beta 1
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).
- Takada, Y. et al. (2007) Genome Biol. 8:215.
- Luo, B-H. et al. (2007) Annu. Rev. Immunol. 25:619.
- Argraves, W.S. et al. (1987) J. Cell Biol. 105:1183.
- Briesewitz, R. et al. (1993) J. Biol. Chem. 268:2989.
- Holers, V.M. et al. (1989) J. Exp. Med. 169:1589.
- Tulla, M. et al. (2001) J. Biol. Chem. 276:48206.
- Eble, J.A. et al. (2006) J. Biol. Chem. 281:25745.
- Hall, D.E. et al. (1990) J. Cell Biol. 110:2175.
- Pozzi, A. et al. (2000) Proc. Natl. Acad. Sci. USA 97:2202.
- Gardner, H. et al. (1999) J. Cell Sci. 112:263.
- Dennis, J. et al. (2010) Am. J. Pathol. 177:2527.
- Cosgrove, D. et al. (2008) Am. J. Pathol. 172:761.
- Chen, X. et al. (2010) Mol. Cell. Biol. 30:3048.
- Borza, C.M. et al. (2010) J. Biol. Chem. 285:40114.
- Gardner, H. et al. (1996) Dev. Biol. 175:301.
- Abair, T.D. et al. (2008) Exp. Cell Res. 314:3593.
Citations for Recombinant Mouse Integrin alpha 1 beta 1 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 3
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Chronic encephalomyelitis virus exhibits cellular tropism and evades pDCs by binding to sialylated integrins as the cell surface receptors
Authors: Takeda, K;Kaifu, T;Michihata, R;Kinugawa, N;Fujioka, A;Tateno, A;Toshima, K;Kanoh, H;Inamori, KI;Kamijo, K;Himeda, T;Ohara, Y;Inokuchi, JI;Nakamura, A;
European journal of immunology
Species: Mouse
Sample Types: Recombinant Protein
Applications: Bioassay -
Group B streptococcus exploits vaginal epithelial exfoliation for ascending infection
Authors: J Vornhagen, B Armistead, V Santana-Uf, C Gendrin, S Merillat, M Coleman, P Quach, E Boldenow, V Alishetti, C Leonhard-M, LY Ngo, C Whidbey, KS Doran, C Curtis, KMA Waldorf, E Nance, L Rajagopal
J. Clin. Invest., 2018-04-09;0(0):.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo -
Proteolytic Isoforms of SPARC Induce Adipose Stromal Cell Mobilization in Obesity.
Authors: Tseng C, Kolonin M
Stem Cells, 2015-09-22;34(1):174-90.
Applications: Bioassay
FAQs
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What is the amino acid sequence of the acidic and basic tails?
Acidic and basic tails are added to the protein to help facilitate optimal activity. While we generally include sequence information on the product datasheet, the sequences of these tails are considered confidential information.
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