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Anti-Laminin β2/γ1 Subunits Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P11047 |
|---|---|
| Host | Mouse |
| Clonality | Mouse Monoclonal |
| Isotype | IgG2b |
| Clone Names | M046 |
| Calculated MW | 177603 Da |
| Gene ID | 3915 |
|---|---|
| Other Names | Laminin subunit gamma-1, Laminin B2 chain Laminin-1 Laminin-10 Laminin-11 Laminin-2 Laminin-3 Laminin-4 Laminin-6 Laminin-7 Laminin-8 Laminin-9 S-laminin S-LAM gamma LAMC1 LAMB2 Laminin 521, Laminin beta 2 |
| Target/Specificity | The human basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains laminin alpha (α), beta (β), and gamma (γ) joined by disulfide bonds. The structure of human laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain including 5 alpha chains, 4 beta chains, and 3 gamma chains. Laminin β2 and γ1 are found in laminin 121, laminin 221, laminin 421, and laminin 521. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Laminin β2/γ1 Subunits Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
The human basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains laminin alpha (α), beta (β), and gamma (γ) joined by disulfide bonds. The structure of human laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain including 5 alpha chains, 4 beta chains, and 3 gamma chains. Laminin β2 and γ1 are found in laminin 121, laminin 221, laminin 421, and laminin 521. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development.
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