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Mouse Anti-Porcine Laminin Gamma 1 (LAMC1) Monoclonal Antibody

Cat. No.VD8N274

Product TypeAnimal-targeted Antibodies

Size

Product Overview

BioVenic mouse monoclonal antibody is specific for laminin gamma 1. It is affinity purified by protein G. It can be applied to WB, IF and ELISA assays of laminin gamma 1.

Specifications

Application WB; IF; ELISA
Clonality Monoclonal
Classification Primary Antibody
Clone G6N18
Host Mouse
Target Species Porcine
Species Reactivity Porcine
Specificity Laminin Gamma 1
Isotype IgG1
Immunogen Recombinant protein of laminin gamma 1
Purification Protein G Purified
Concentration 500 μg/mL
Conjugation Unconjugated
Preservative and Stabilizer 0.02% Sodium Azide
Buffer Phosphate Buffered Saline with 50% Glycerol, pH 7.3
Physical State Liquid

Target Information

Porcine laminin gamma 1 (LAMC1) is a critical component of the laminin family of proteins, which are essential structural elements of the extracellular matrix (ECM) in pigs. Laminins are multimeric glycoproteins that contribute to the formation of basement membranes, providing support and stability to cells and tissues. LAMC1, in particular, combines with other laminin chains to form laminin-5, a crucial isoform that plays a significant role in cell adhesion, migration, and differentiation. It is highly involved in tissue development, wound healing, and the maintenance of tissue integrity, particularly in epithelial and endothelial tissues.

Target Laminin Gamma 1
Target Synonym LAMB2; LAMC1
Gene ID 100514785
UniProt ID A0A4X1TYI6

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C (up to 12 months) on receipt.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Lössl, Philip, et al. "Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes." Plos one 9.11 (2014): e112886.
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