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ITGA7 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, FC, IHC-P, IF, E |
|---|---|
| Primary Accession | Q13683 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 128948 Da |
| Antigen Region | 247-279 aa |
| Gene ID | 3679 |
|---|---|
| Other Names | Integrin alpha-7, Integrin alpha-7 heavy chain, Integrin alpha-7 light chain, Integrin alpha-7 70 kDa form, ITGA7 |
| Target/Specificity | This ITGA7 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 247-279 amino acids from the N-terminal region of human ITGA7. |
| Dilution | IF~~1:25 WB~~1:2000 IHC-P~~1:25 FC~~1:25 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ITGA7 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ITGA7 |
|---|---|
| Function | Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as a Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. |
| Cellular Location | Membrane; Single-pass type I membrane protein. |
| Tissue Location | Isoforms containing segment A are predominantly expressed in skeletal muscle. Isoforms containing segment B are abundantly expressed in skeletal muscle, moderately in cardiac muscle, small intestine, colon, ovary and prostate and weakly in lung and testes. Isoforms containing segment X2D are expressed at low levels in fetal and adult skeletal muscle and in cardiac muscle, but are not detected in myoblasts and myotubes. In muscle fibers isoforms containing segment A and B are expressed at myotendinous and neuromuscular junctions; isoforms containing segment C are expressed at neuromuscular junctions and at extrasynaptic sites. Isoforms containing segments X1 or X2 or, at low levels, X1X2 are expressed in fetal and adult skeletal muscle (myoblasts and myotubes) and cardiac muscle |
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Provided below are standard protocols that you may find useful for product applications.
Background
Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells.
References
Leung E.,et al.Biochem. Biophys. Res. Commun. 243:317-325(1998).
Hayashi Y.K.,et al.Nat. Genet. 19:94-97(1998).
Vizirianakis I.S.,et al.Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
Vignier N.,et al.Biochem. Biophys. Res. Commun. 260:357-364(1999).
Clark H.F.,et al.Genome Res. 13:2265-2270(2003).
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