antibody

Laminin antibody

MBS830149

0.1 ml

420 USD

monoclonal

mouse

nonconjugated

2D9G5

western blot, ELISA, enzyme immunoassay

Antibody

Laminin antibody

Laminin

Monoclonal Laminin; Anti-Laminin; Laminin A chain; Laminin alpha 1 chain; LAMB1; LAMA1; Laminin alpha 1; Anti Laminin; Laminin B1 chain; Laminin subunit beta 1; Laminin

Laminin; Laminin subunit gamma-2; laminin subunit gamma-2; laminin, gamma 2; Cell-scattering factor 140 kDa subunit; CSF 140 kDa subunit; Epiligrin subunit gamma; Kalinin subunit gamma; Kalinin/nicein/epiligrin 100 kDa subunit; Ladsin 140 kDa subunit; Laminin B2t chain; Laminin-5 subunit gamma; Large adhesive scatter factor 140 kDa subunit; Nicein subunit gamma

LAMC2; LAMC2; B2T; CSF; EBR2; BM600; EBR2A; LAMB2T; LAMNB2; LAMB2T; LAMNB2; CSF 140 kDa subunit

LAMC2_HUMAN

Monoclonal

IgG2a

2D9G5

Mouse

Human

1193

Supplied as a liquid in ascitic fluid containing 0.03% sodium azide.

1.0 mg/ml

Store at 4 degree C for short term storage. Store at -20 degree C for long term storage. Avoid repeated freeze/thaw cycles.

ELISA (EIA), Western Blot (WB)

ELISA: 1:10,000. WB: 1:500-1:2000

Biological Significance: Laminins are major proteins in the basal lamina, a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, adhesion as well as phenotype and survival.

Immunogen: Laminin antibody was raised in Mouse using a purified recombinant fragment of Laminin(aa31-270) expressed in E Coli as the immunogen.

Cell Biology

Mouse monoclonal Laminin antibody

34230

CAA78728.1

Q13753

121,604 Da

Alpha6-Beta4 Integrin Signaling Pathway 198807!!Amoebiasis Pathway 167324!!Amoebiasis Pathway 167191!!Anchoring Fibril Formation Pathway 730307!!Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway 730306!!Cell Junction Organization Pathway 160966!!Cell-Cell Communication Pathway 477132!!Collagen Formation Pathway 645288!!Degradation Of The Extracellular Matrix Pathway 576263!!ECM-receptor Interaction Pathway 83068

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease characterized by blisters due to disruption of the epidermal-dermal junction. Two transcript variants resulting from alternative splicing of the 3' terminal exon, and encoding different isoforms of gamma 2 chain, have been described. The two variants are differentially expressed in embryonic tissues, however, the biological significance of the two forms is not known. Transcript variants utilizing alternative polyA_signal have also been noted in literature. [provided by RefSeq, Aug 2011]

0.1 ml

420 USD