A part of Merck

MAB1922 | Anti-Laminin α2 Antibody, clone 5H2

100 µL  
Recuperando precio...
No pudo obtenerse el precio
La cantidad mínima tiene que ser múltiplo de
Al finalizar el pedido Más información
Ahorró ()
Solicitar precio
Disponibilidad a confirmarDisponibilidad a confirmar
En existencia 
Cantidades limitadas disponibles
Debe confirmarse disponibilidad
    El resto: se avisará
      El resto: se avisará
      Se avisará
      Póngase en contacto con el Servicio de Atención al Cliente

      Ofertas especiales


      Póngase en contacto con el Servicio de Atención al Cliente

      Click To Print This Page


      Replacement Information

      Ofertas especiales

      Tabla espec. clave

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, Mk, Rb ELISA, CULT, IF, IHC, IP, WB M Ascites Monoclonal Antibody
      Catalogue NumberMAB1922
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Laminin α2 Antibody, clone 5H2
      Alternate Names
      • Laminin M chain
      • Merosin heavy chain
      • laminin M
      • laminin alpha 2 subunit
      • laminin, alpha 2
      Background InformationElements of the extracellular matrix such as laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in organs including the kidney, lung, skin, and nervous system. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. For example, the alpha subfamily of laminin chains is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined. At least 15 distinct laminin trimers, containing various combinations of 5 alpha, 4 beta, and 3 gamma subunits have been found in mammals. Both laminin alpha 5 and alpha 1 are prevalent in kidney. Mice that are homozygous for a null mutation in the alpha 5 laminin gene are dead by embrionic day 14 - 19 with multiple developmental abnormalities. The kidney phenotypes include avascular glomeruli, impaired branching morphogenesis, and renal agenesis.
      Product Information
      • Vascular breast carcinomas, Cultured embryonic retinal neurons and RGCs
      PresentationUnpurified ascites in buffer containing no preservatives.
      ApplicationDetect Laminin α2 using this Anti-Laminin α2 Antibody, clone 5H2 validated for use in ELISA, CULT, IF, IH, IP & WB.
      Key Applications
      • ELISA
      • Cell Culture
      • Immunofluorescence
      • Immunohistochemistry
      • Immunoprecipitation
      • Western Blotting
      Application NotesELISA:
      50% maximal binding to human merosin at 1:50,000 dilution from a previous lot.

      1:5,000 dilution from a previous lot was used for staining of 8 µm acetone-fixed cryostat muscle sections, prior to detection with a peroxidase-conjugated secondary antibody.

      A previous lot of this antibody was used in immunofluorescent.

      Affinity chromatography:
      A previous lot of this antibody was used in IAP.

      A previous lot of this antibody was used in IP.

      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenPurified human merosin
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityReacts with the 80 kDa fragment of the M-chain of human merosin.
      Species Reactivity
      • Human
      • Monkey
      • Rabbit
      Species Reactivity NoteCross reacts with monkey and rabbit merosin.
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryLaminin, an extracellular protein, is a major component of the basement membrane. It is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. It is composed of three subunits, alpha, beta, and gamma, which are bound to each other by disulfide bonds into a cross-shaped molecule. This gene encodes the alpha 2 chain, which constitutes one of the subunits of laminin 2 (merosin) and laminin 4 (s-merosin). Mutations in this gene have been identified as the cause of congenital merosin-deficient muscular dystrophy. Two transcript variants encoding different proteins have been found for this gene.
      Gene Symbol
      • LAMA2
      • LAMM
      Purification MethodUnpurified
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P24043 # Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
      SIZE: 3110 amino acids; 342771 Da
      SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (merosin) and laminin-4 (S- merosin).
      SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
      TISSUE SPECIFICITY: Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.
      DOMAIN: SwissProt: P24043 The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. & Domains VI, IV and G are globular.
      DISEASE: SwissProt: P24043 # Defects in LAMA2 are the cause of merosin-deficient congenital muscular dystrophy type 1A (MDC1A) [MIM:607855]. MDC1A is characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.
      SIMILARITY: Contains 17 laminin EGF-like domains. & Contains 5 laminin G-like domains. & Contains 2 laminin IV type A domains. & Contains 1 laminin N-terminal domain.
      Molecular Weight80 kDa
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceRoutinely evaluated by Western Blot on Human Placenta lysate.

      Western Blot Analysis:
      1:1000 dilution of this lot detected Laminin α2 (merosin) on 10 μg of Human Placenta lysate.
      Usage Statement
      • 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.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at -20ºC from date of receipt.
      Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage the IgG1 and affect product performance.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information


      Ficha datos de seguridad (MSDS)


      Ficha técnica de seguridad del material (MSDS) 

      Certificados de análisis

      CargoNúmero de lote
      Anti-Laminin #225;2, clone 5H2 - LV1496265 LV1496265
      Anti-Laminin 2, clone 5H2 - LV1624582 LV1624582
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2465241 2465241
      Anti-Laminin alpha2 [Merosin], -2549088 2549088
      Anti-Laminin alpha2 [Merosin], -2574073 2574073
      Anti-Laminin alpha2 [Merosin], -2660698 2660698
      Anti-Laminin alpha2 [Merosin], -2697560 2697560
      Anti-Laminin alpha2 [Merosin], -2726799 2726799
      Anti-Laminin alpha2 [Merosin], -2776770 2776770
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 1984678 1984678
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2029622 2029622
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2037175 2037175
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2058330 2058330
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2090931 2090931
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2276342 2276342
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2327467 2327467
      Anti-Laminin alpha2 [Merosin], clone 5H2 - 2828586 2828586
      Anti-Laminin alpha2 [Merosin], clone 5H2 - LV1624582 LV1624582
      Anti-Laminin alpha2 [Merosin], clone 5H2 - LV1675705 LV1675705
      Anti-Laminin alpha2 [Merosin], clone 5H2 - LV1739982 LV1739982
      Anti-Laminin alpha2 [Merosin], clone 5H2 - LV1777797 LV1777797
      Anti-Laminin alpha2 [Merosin], clone 5H2 - NG1857577 NG1857577
      Anti-Laminin alpha2 [Merosin], clone 5H2 -2506447 2506447

      Referencias bibliográficas | 38 Disponible | Ver todas las referencias

      Visión general referenciasAplicación EspeciePub Med ID
      Resistance exercise increases active MMP and β1-integrin protein expression in skeletal muscle.
      Ogasawara, R; Nakazato, K; Sato, K; Boppart, MD; Fujita, S
      Physiological reports 2 2014

      Mostrar resumen
      25413329 25413329
      ISPD gene mutations are a common cause of congenital and limb-girdle muscular dystrophies.
      Cirak, S; Foley, AR; Herrmann, R; Willer, T; Yau, S; Stevens, E; Torelli, S; Brodd, L; Kamynina, A; Vondracek, P; Roper, H; Longman, C; Korinthenberg, R; Marrosu, G; Nürnberg, P; , ; Michele, DE; Plagnol, V; Hurles, M; Moore, SA; Sewry, CA; Campbell, KP; Voit, T; Muntoni, F
      Brain : a journal of neurology 136 269-81 2013

      Mostrar resumen
      ImmunohistochemistryHuman23288328 23288328
      Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of α-dystroglycan.
      Stevens, E; Carss, KJ; Cirak, S; Foley, AR; Torelli, S; Willer, T; Tambunan, DE; Yau, S; Brodd, L; Sewry, CA; Feng, L; Haliloglu, G; Orhan, D; Dobyns, WB; Enns, GM; Manning, M; Krause, A; Salih, MA; Walsh, CA; Hurles, M; Campbell, KP; Manzini, MC; , ; Stemple, D; Lin, YY; Muntoni, F
      American journal of human genetics 92 354-65 2013

      Mostrar resumen
      Immunohistochemistry23453667 23453667
      Clinical and molecular characterization of limb-girdle muscular dystrophy due to LAMA2 mutations.
      Gavassini BF, Carboni N, Nielsen JE, Danielsen ER, Thomsen C, Svenstrup K, Bello L, Maioli MA, Marrosu G, Ticca AF, Mura M, Marrosu MG, Soraru G, Angelini C, Vissing J, Pegoraro E.
      Muscle & nerve 44 703-9 2011

      Mostrar resumen
      21953594 21953594
      The contribution of human synovial stem cells to skeletal muscle regeneration.
      Meng J, Adkin CF, Arechavala-Gomeza V, Boldrin L, Muntoni F, Morgan JE
      Neuromuscul Disord 20 6-15. 2010

      Mostrar resumen
      20034794 20034794
      Immunohistochemical analysis of calpain 3: advantages and limitations in diagnosing LGMD2A.
      Richard Charlton,Matthew Henderson,Julie Richards,Judith Hudson,Volker Straub,Kate Bushby,Rita Barresi
      Neuromuscular disorders : NMD 19 2009

      Mostrar resumen
      19556129 19556129
      A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity.
      Cecilia Jimenez-Mallebrera,Silvia Torelli,Lucy Feng,Jihee Kim,Caroline Godfrey,Emma Clement,Rachael Mein,Stephen Abbs,Susan C Brown,Kevin P Campbell,Stephan Kröger,Beril Talim,Haluk Topaloglu,Ros Quinlivan,Helen Roper,Anne M Childs,Maria Kinali,Caroline A Sewry,Francesco Muntoni
      Brain pathology (Zurich, Switzerland) 19 2009

      Mostrar resumen Artículo Texto completo
      18691338 18691338
      Diagnosis and etiology of congenital muscular dystrophy.
      R A Peat, J M Smith, A G Compton, N L Baker, R A Pace, D J Burkin, S J Kaufman, S R Lamandé, K N North
      Neurology 71 312-21 2008

      Mostrar resumen
      18160674 18160674
      Mild POMGnT1 mutations underlie a novel limb-girdle muscular dystrophy variant.
      Clement, EM; Godfrey, C; Tan, J; Brockington, M; Torelli, S; Feng, L; Brown, SC; Jimenez-Mallebrera, C; Sewry, CA; Longman, C; Mein, R; Abbs, S; Vajsar, J; Schachter, H; Muntoni, F
      Archives of neurology 65 137-41 2008

      Mostrar resumen
      18195152 18195152
      Mutations in contactin-1, a neural adhesion and neuromuscular junction protein, cause a familial form of lethal congenital myopathy.
      Alison G Compton,Douglas E Albrecht,Jane T Seto,Sandra T Cooper,Biljana Ilkovski,Kristi J Jones,Daniel Challis,David Mowat,Barbara Ranscht,Melanie Bahlo,Stanley C Froehner,Kathryn N North
      American journal of human genetics 83 2008

      Mostrar resumen Artículo Texto completo
      19026398 19026398

      Ficha técnica

      Anti-Laminin alpha2, clone 5H2 - Data Sheet