ALEXIS Biochemicals: Monoclonal Antibody to Laminin-2 (α-2-chain) (4H8-2)

ALX-804-190

Revised 21-Aug-08

Monoclonal Antibody to Laminin-2 (α-2-chain) (4H8-2)
SYNONYMS	anti-Merosin MAb (4H8-2) LAMA2
PRODUCT LINE	Cytoskeleton
PRODUCT CATEGORY	Laminin / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
ALX-804-190-C100		100 µg	309.00 USD

Product Specification

SPECIES CROSSREACTIVITY:	Human Mouse
CLONE:	4H8-2
ISOTYPE:	Rat IgG1
PURITY DETAIL:	Purified from serum-free cell culture supernatant by subsequent thiophilic adsorption and size exclusion chromatography.
FORMULATION:	Lyophilized from 1ml 2x PBS, 0.09% sodium azide, PEG and sucrose.
RECONSTITUTION:	Reconstitute with 1ml distilled water (15 min, RT).
IMMUNOGEN:	Mouse heart laminin-2 (merosin).
SPECIFICITY:	Recognizes human and mouse laminin α2 (300kDa). Recognizes an N-terminal portion of the α2 chain that is deleted in congenital muscular dystrophies.
APPLICATION:	ELISA (0.02-0.1µg/ml) Immunohistochemistry Immunoprecipitation (use at 1-10µg/ml in PBS) Note: Not recommended for Western blot.
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C
USE/STABILITY:	Reconstituted antibody is stable for 1 year when stored at -80°C. Thaw aliquots at +37°C. Thawed aliquots may be stored at +4°C for up to 3 months.
HANDLING:	Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and freeze in liquid nitrogen.

Product Specific Literature References

Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo: F. Schuler & L.M. Sorokin; J. Cell Sci. 108, 3795 (1995) Abstract; Full Text
Diagnosis of merosin (laminin-2) deficient congenital muscular dystrophy by skin biopsy: C.A. Sewry, et al.; Lancet 347, 582 (1996) Abstract
Mild congenital muscular dystrophy in two patients with an internally deleted laminin alpha2-chain: V. Allamand, et al.; Hum. Mol. Gen. 6, 747 (1997) Abstract; Full Text
Loss of the sarcoglycan complex and sarcospan leads to muscular dystrophy in beta-sarcoglycan-deficient mice: K. Araishi, et al.; Hum. Mol. Genet. 8, 1589 (1999) Abstract; Full Text
Characterization of bone marrow laminins and identification of alpha5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells: Y. Gu, et al.; Blood 93, 2533 (1999) Abstract; Full Text
Skeletal muscle engraftment potential of adult mouse skin side population cells: F. Montanaro, et al.; PNAS 100, 9336 (2003) Abstract; Full Text
Laminins alpha2 and alpha4 in pancreatic acinar basement membranes are required for basal receptor localization: J.H. Miner, et al.; J. Histochem. Cytochem. 52, 153 (2004) Abstract; Full Text
Laminin alpha2 is essential for odontoblast differentiation regulating dentin sialoprotein expression: K. Yuasa, et al.; J. Biol. Chem. 279, 10286 (2004) Abstract; Full Text
Lung development in laminin gamma2 deficiency: abnormal tracheal hemidesmosomes with normal branching morphogenesis and epithelial differentiation: N.M. Nguyen, et al.; Respir.Res. 7, 28 (2006) Abstract; Full Text
A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination: BL. Patton, et al.; J. Cell Sci. 121, 1593 (2008) Abstract
Hematopoietic Contribution to Skeletal Muscle Regeneration in Acid Alpha-glucosidase Knockout Mice.: J. Mori, et al.; J. Histochem. Cytochem. 56, 811 (2008) Abstract

General Information

The laminins are a family of glycoproteins that provide an integral part of the structural scaffolding of basement membranes in almost every tissue. Each laminin is a heterotrimer assembled from α, β and γ chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycans, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, cell shape and movement, maintenance of tissue phenotypes and promotion of tissue survival.

General Literature References

Form and function: the laminin family of heterotrimers: H. Colognato & P.D. Yurchenko; Dev. Dyn. 218, 213 (2000), (Review) Abstract; Full Text
Laminin: the crux of basement membrane assembly: T. Sasaki, et al.; J. Cell Biol. 164, 959 (2004), (Review) Abstract; Full Text
Laminin-induced signaling in tumor cells: V. Givant-Horwitz, et al.; Cancer Lett. 223, 1 (2005), (Review) Abstract
Physiological and pathological implications of laminins: from the gene to the protein: M.C. Paez, et al.; Autoimmunity 40, 83 (2007), (Review) Abstract