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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Conjugate:
unconjugated
Clone:
4H8-2, monoclonal
Application:
ARR, ELISA (i), ICC, IF, IHC (f), IP, WB
Citations:
104
biological source
rat
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
4H8-2, monoclonal
form
buffered aqueous solution
mol wt
antigen ~400 kDa (denatured)
species reactivity
human, mouse
packaging
antibody small pack of 25 μL
concentration
~2 mg/mL
technique(s)
immunocytochemistry: suitable, immunohistochemistry (frozen sections): suitable, immunoprecipitation (IP): suitable, indirect ELISA: suitable, indirect immunofluorescence: 4-8 μg/mL using acetone-fixed frozen sections of human tongue, microarray: suitable, western blot: suitable
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... LAMA2(3908)
mouse ... Lama2(16773)
General description
The gene LAMA2 (laminin-2) encodes a protein belonging to a large family of heterotrimeric glycoproteins called laminins. It contains a large globular C-terminal domain that binds to dystroglycan and integrin α7β1 cell receptor specific for myofibers. The amino terminal domain associates with other laminins during the formation of protein meshwork that is involved in the basal membrane supramolecular assembly. The gene is mapped to human chromosome 6q22.33.
Laminin, the most abundant structural and biologically active component in basement membrane, is a complex extracellular glycoprotein of 700-900 kDa that plays an important role in many aspects of the cell biology. It is composed of one α chain (approx. 400 kDa, previously called A chain) one β chain (215 kDa, B1) and one γ chain (205 kDa, B2), held together by disulfide bonds.
Anti-Laminin-2 (α-2 Chain) antibody, Rat monoclonal (rat IgG1 isotype) is derived from the 4H8-2 hybridoma produced by the fusion of rat myeloma cells and splenocytes from a Lewis rat immunized with mouse heart laminin-2.1 The antibody is purified from the culture supernatant of hybridoma cells grown in a bioreactor. Anti-Laminin-2 (α-2 Chain) antibody, Rat monoclonal reacts specifically with mouse1 and human2, laminin-2. The epitope recognized by the antibody resides in the N-terminal portion of the α2 chain of laminin.
Laminin, the most abundant structural and biologically active component in basement membrane, is a complex extracellular glycoprotein of 700-900 kDa that plays an important role in many aspects of the cell biology. It is composed of one α chain (approx. 400 kDa, previously called A chain) one β chain (215 kDa, B1) and one γ chain (205 kDa, B2), held together by disulfide bonds.
Anti-Laminin-2 (α-2 Chain) antibody, Rat monoclonal (rat IgG1 isotype) is derived from the 4H8-2 hybridoma produced by the fusion of rat myeloma cells and splenocytes from a Lewis rat immunized with mouse heart laminin-2.1 The antibody is purified from the culture supernatant of hybridoma cells grown in a bioreactor. Anti-Laminin-2 (α-2 Chain) antibody, Rat monoclonal reacts specifically with mouse1 and human2, laminin-2. The epitope recognized by the antibody resides in the N-terminal portion of the α2 chain of laminin.
Immunogen
Mouse heart laminin-2
Application
Anti-Laminin-2 (α-2 Chain) antibody, Rat monoclonal has been used in immunofluorescence and immunohistochemistry.
Biochem/physiol Actions
Laminins are glycoproteins that function in extracellular matrix architecture, cell adhesion, differentiation, and neurite outgrowth. Mutations in the gene LAMA2 (laminin-2) leading to either partial deficiency or complete absence of laminin α2 have been associated with limb-girdle muscular dystrophy (LGMD), characterized by severe, early-onset congenital muscular dystrophy to mild, later childhood-onset limb-girdle type muscular dystrophy, hypotonia with muscle weakness at early infancy, poor spontaneous movements with contractures of the large joints, and weak cry along with respiratory dysfunction.
The epitope recognized by the antibody resides in the N-terminal portion of the α2 chain of laminin.
Physical form
Solution in phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in "frostfree" freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
Purified from the culture supernatant of hybridoma cells grown in a bioreactor.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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저장 등급
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Skeletal Muscle Tissue Clearing for LacZ and Fluorescent Reporters, and Immunofluorescence Staining.
Verma M
Methods in Molecular Biology, 1460, 129-140 (2016)
Expression and distribution of laminin a1 and a2 chains in embryonic and adult mouse tissues: an immunochemical approach.
Sasaki T, et al.
Experimental Cell Research, 275(2), 185-199 (2002)
The role of pericytic laminin in blood brain barrier integrity maintenance.
Gautam J, et.al.
Scientific Reports, 6, 36450-36450 (2016)
Thomas C Roberts et al.
Nucleic acids research, 41(20), 9500-9513 (2013-08-16)
Extracellular microRNAs (miRNAs) are promising biomarkers of the inherited muscle wasting condition Duchenne muscular dystrophy, as they allow non-invasive monitoring of either disease progression or response to therapy. In this study, serum miRNA profiling reveals a distinct extracellular miRNA signature
Clinical and molecular characterization of limb-girdle muscular dystrophy due to LAMA2 mutations.
Gavassini BF
Muscle and Nerve, 44, 703-709 (2011)
관련 콘텐츠
Instructions
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