D5

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$40.00
SKU: D5
View product citations for antibody D5 on CiteAb

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DSHB Data Sheet

Catalog Fields

Antigen: laminin, beta-2
Hybridoma Cells Available: Yes
Antigen Species: Bovine
Depositor: Sanes, J.R.
Isotype: MIgG1
Antigen Sequence:
Host Species: mouse
Depositors Institution: Harvard University
Positive Tested Species Reactivity: Canine, Guinea Pig, Rabbit, Rat
Depositors Notes: D5 blocks binding of neurons to s-laminin fusion protein.
Antigen Molecular Weight: Predicted: 192 kDa; Apparent: 190 kDa (reducing conditions)
Human Protein Atlas:  
Predicted Species Reactivity:  
Gene: LAMB2
Immunogen: Adult bovine anterior lens capsule
Alternate Gene Names: LAMS
Alternate Antibody Name:
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped: Yes
Myeloma Strain: fox NY
Epitope Location or Sequence: C-terminal, domain I region
Uniprot ID: E1BDK6 
Immunogen Sequence: full length protein
Entrez Gene ID: 520167 
Additional Characterization:  
Antibody Registry ID: AB_528329 
Additional Information: The former name of laminin beta-2 was S-laminin. D5 doesn't cross-react with mouse antigen. C4, D5 and D7 recognize different epitopes.
Recommended Applications: Function Blocking, Immunofluorescence, Immunoprecipitation, Western Blot
These hybridomas were created by your colleagues. Please acknowledge the hybridoma contributor and the Developmental Studies Hybridoma Bank (DSHB) in the Materials and Methods of your publications. Please email the citation to us.
For your Materials & Methods section:
D5 was deposited to the DSHB by Sanes, J.R. (DSHB Hybridoma Product D5)
Storage and Handling Recommendations
Although many cell products are maintained at 4°C for years without loss of activity, shelf-life at 4°C is highly variable. For immediate use, short term storage at 4°C up to two weeks is recommended. For long term storage, divide the solution into volumes of no less than 20 ul for freezing at -20°C or -80°C. The small volume aliquot should provide sufficient reagent for short term use. Freeze-thaw cycles should be avoided. For concentrate or bioreactor products, an equal volume of glycerol, a cryoprotectant, may be added prior to freezing.
Usage Recommendations
Although the optimal Ig concentration for an application varies for each product and must be optimized for each laboratory, a good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) is 2-5 ug/ml. For western blots, the recommended concentration range is 0.2-0.5 ug/ml.
All cell products contain the antimicrobial ProClin. Click here for additional information.

14 References

  • Initial Publication
  • IF References
  • WB References
  • IP References
  • FB References
  • Epitope Map References
  • All References
  • Initial Publication

    The basal lamina of the neuromuscular junction.
    Chiu AY
    Cold Spring Harbor symposia on quantitative biology 48 Pt 2. (1983): 667-78.

    IF References

    A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction.
    Sanes JR
    Nature 338.6212 (1989 Mar 16): 229-34.

    Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere.
    Hunter DD
    The Journal of cell biology 111.4 (1990 Oct): 1685-99.

    Expression of s-laminin and laminin in the developing rat central nervous system.
    Sanes JR
    The Journal of comparative neurology 323.2 (1992 Sep 8): 238-51.

    A synaptic localization domain in the synaptic cleft protein laminin beta 2 (s-laminin)
    Sanes JR
    Science (New York, N.Y.) 269.5222 (1995 Jul 21): 413-6.

    Characterization of bone marrow laminins and identification of alpha5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells.
    Ekblom M
    Blood 93.8 (1999 Apr 15): 2533-42.

    Differential laminin isoform expression in the developing rat olfactory system.
    Schwarting GA
    Brain research. Developmental brain research 101.1-2 (1997 Jul 18): 187-96.

    Composition in situ and in vitro of vascular smooth muscle laminin in the rat.
    McGuffee LJ
    Cell and tissue research 281.1 (1995 Jul): 187-96.

    S-laminin and N-acetylgalactosamine located at the synaptic basal lamina of skeletal muscle are involved in synaptic recognition by growing neurites.
    Comella JX
    Journal of neurocytology 24.12 (1995 Dec): 903-15.

    Diabetes induces changes in glomerular development and laminin-beta 2 (s-laminin) expression.
    Abrahamson DR
    The American journal of pathology 151.4 (1997 Oct): 1131-40.

    A missense LAMB2 mutation causes congenital nephrotic syndrome by impairing laminin secretion.
    Miner JH
    Journal of the American Society of Nephrology : JASN 22.5 (2011 May): 849-58.

    WB References
    IP References

    Synthesis and assembly of the synaptic cleft protein S-laminin by cultured cells.
    Sanes JR
    The Journal of biological chemistry 267.3 (1992 Jan 25): 2014-22.

    FB References

    A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction.
    Sanes JR
    Nature 338.6212 (1989 Mar 16): 229-34.

    S-laminin and N-acetylgalactosamine located at the synaptic basal lamina of skeletal muscle are involved in synaptic recognition by growing neurites.
    Comella JX
    Journal of neurocytology 24.12 (1995 Dec): 903-15.

    An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to S-laminin.
    Sanes JR
    The Journal of neuroscience : the official journal of the Society for Neuroscience 11.12 (1991 Dec): 3960-71.

    Epitope Map References
    All References

    A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction.
    Sanes JR
    Nature 338.6212 (1989 Mar 16): 229-34.

    Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere.
    Hunter DD
    The Journal of cell biology 111.4 (1990 Oct): 1685-99.

    Expression of s-laminin and laminin in the developing rat central nervous system.
    Sanes JR
    The Journal of comparative neurology 323.2 (1992 Sep 8): 238-51.

    A synaptic localization domain in the synaptic cleft protein laminin beta 2 (s-laminin)
    Sanes JR
    Science (New York, N.Y.) 269.5222 (1995 Jul 21): 413-6.

    Characterization of bone marrow laminins and identification of alpha5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells.
    Ekblom M
    Blood 93.8 (1999 Apr 15): 2533-42.

    Differential laminin isoform expression in the developing rat olfactory system.
    Schwarting GA
    Brain research. Developmental brain research 101.1-2 (1997 Jul 18): 187-96.

    Composition in situ and in vitro of vascular smooth muscle laminin in the rat.
    McGuffee LJ
    Cell and tissue research 281.1 (1995 Jul): 187-96.

    S-laminin and N-acetylgalactosamine located at the synaptic basal lamina of skeletal muscle are involved in synaptic recognition by growing neurites.
    Comella JX
    Journal of neurocytology 24.12 (1995 Dec): 903-15.

    Diabetes induces changes in glomerular development and laminin-beta 2 (s-laminin) expression.
    Abrahamson DR
    The American journal of pathology 151.4 (1997 Oct): 1131-40.

    A missense LAMB2 mutation causes congenital nephrotic syndrome by impairing laminin secretion.
    Miner JH
    Journal of the American Society of Nephrology : JASN 22.5 (2011 May): 849-58.

    Purification and lectin-binding properties of s-laminin, a synaptic isoform of the laminin B1 chain.
    Ko J
    Journal of neurochemistry 59.1 (1992 Jul): 10-7.

    Synthesis and assembly of the synaptic cleft protein S-laminin by cultured cells.
    Sanes JR
    The Journal of biological chemistry 267.3 (1992 Jan 25): 2014-22.

    An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to S-laminin.
    Sanes JR
    The Journal of neuroscience : the official journal of the Society for Neuroscience 11.12 (1991 Dec): 3960-71.

    The basal lamina of the neuromuscular junction.
    Chiu AY
    Cold Spring Harbor symposia on quantitative biology 48 Pt 2. (1983): 667-78.

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