Description

  • Product name

    Recombinant Human LAMA3 protein
  • Expression system

    Wheat germ
  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      SSQQQRVPFLQPPGQSQLQASYVEFRPSQGCSPGYYRDHKGLYTGRCVPC NCNGHSNQCQDGSGICVNCQHNTAGEHCERCQEGYYGNAVHGSCRACPCP HTNSFATGCV
    • Amino acids

      29 to 138
    • Tags

      GST tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab158810 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    ELISA

    Western blot

  • Form

    Liquid
  • Additional notes

    Protein concentration is above or equal to 0.05 mg/ml.

     This product was previously labelled as Laminin subunit alpha-3, Laminin 5 alpha 3

     

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names

    • E170
    • Epiligrin 170 kDa subunit
    • Epiligrin subunit alpha
    • Kalinin B1 chain
    • Kalinin subunit alpha
    • LAMA3
    • LAMA3_HUMAN
    • LAMB3
    • LAMC2
    • Laminin gamma 2
    • Laminin 5 beta 3
    • Laminin 5 gamma 2 subunit
    • Laminin beta 3
    • Laminin subunit alpha-3
    • Laminin subunit beta 3
    • Laminin subunit gamma 2
    • Laminin-5 subunit alpha
    • Laminin-6 subunit alpha
    • Laminin-7 subunit alpha
    • Nicein subunit alpha
    see all
  • Function

    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.
    Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes.
  • Tissue specificity

    Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.
  • Involvement in disease

    Defects in LAMA3 are a cause of epidermolysis bullosa junctional Herlitz type (H-JEB) [MIM:226700]; also known as junctional epidermolysis bullosa Herlitz-Pearson type. JEB defines a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement membrane. H-JEB is a severe, infantile and lethal form. Death occurs usually within the first six months of life. Occasionally, children survive to teens. H-JEB is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
    Defects in LAMA3 are the cause of laryngoonychocutaneous syndrome (LOCS) [MIM:245660]. LOCS is an autosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx.
  • Sequence similarities

    Contains 15 laminin EGF-like domains.
    Contains 5 laminin G-like domains.
    Contains 1 laminin IV type A domain.
    Contains 1 laminin N-terminal domain.
  • Domain

    The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
    Domain G is globular.
  • Cellular localization

    Secreted > extracellular space > extracellular matrix > basement membrane. Major component.
  • Information by UniProt

Images

  • ab158810 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab158810 has not yet been referenced specifically in any publications.

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