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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human CD29/ITGB1 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 44.26 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Ser86-Ile461 |
Aliases /Synonyms | MSK12, VLA-4 subunit beta, CD29, Integrin beta-1, ITGB1, FNRB, MDF2, GPIIA, Glycoprotein IIa, Fibronectin receptor subunit beta |
Reference | ARO-P11876 |
Note | For research use only. |
The recombinant human CD29/ITGB1 protein is a key component of the integrin family, which are cell surface receptors involved in cell adhesion and signaling. This protein is also known as the beta-1 integrin subunit, and it plays a crucial role in various cellular processes such as cell migration, proliferation, and differentiation. In this article, we will discuss the structure, activity, and application of this important protein.
The recombinant human CD29/ITGB1 protein is a transmembrane glycoprotein that is composed of a large extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain is made up of seven beta-strands and a large alpha-helical domain, which are connected by flexible loops. This structure allows the protein to interact with other proteins and molecules on the cell surface.
The transmembrane domain of CD29/ITGB1 is responsible for anchoring the protein to the cell membrane, while the cytoplasmic tail is involved in intracellular signaling. The cytoplasmic tail contains binding sites for various signaling molecules, which allows the protein to transmit signals from the extracellular environment to the inside of the cell.
The activity of the recombinant human CD29/ITGB1 protein is primarily related to its role in cell adhesion and signaling. This protein is known to interact with a wide range of extracellular matrix proteins, such as fibronectin, collagen, and laminin, through its extracellular domain. This interaction is crucial for the attachment of cells to the extracellular matrix, which is essential for cell migration, tissue organization, and wound healing.
In addition to its role in cell adhesion, CD29/ITGB1 also plays a significant role in cell signaling. The cytoplasmic tail of this protein can interact with various signaling molecules, including kinases and adaptor proteins, which allows it to regulate cellular processes such as cell proliferation, survival, and differentiation.
The recombinant human CD29/ITGB1 protein has various applications in both research and clinical settings. One of the primary uses of this protein is in the study of cell adhesion and migration. Researchers can use recombinant CD29/ITGB1 to investigate the role of this protein in different cellular processes and to understand its interactions with other proteins and molecules.
In clinical settings, recombinant CD29/ITGB1 has been used in the development of novel therapeutics. For example, this protein has been used in the design of drugs that target integrin-mediated signaling pathways, which are involved in various diseases such as cancer, autoimmune disorders, and cardiovascular diseases. In addition, recombinant CD29/ITGB1 has also been used in tissue engineering and regenerative medicine, where it is used to promote cell adhesion and tissue repair.
In summary, the recombinant human CD29/ITGB1 protein is a crucial component of the integrin family, and it plays a vital role in cell adhesion and signaling. Its structure, activity, and application make it an essential protein for both research and clinical purposes. Further studies on this protein will continue to enhance our understanding of its role in cellular processes and its potential as a therapeutic target.
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