6F1

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$40.00
SKU: 6F1-s
View product citations for antibody 6F1 on CiteAb

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DSHB Data Sheet

Catalog Fields

Antigen: integrin alpha-2 (CD49B), human
Hybridoma Cells Available:
Antigen Species: Human
Depositor: Coller, B.S.
Isotype: MIgG1
Antigen Sequence:
Host Species: mouse
Depositors Institution: Rockefeller University
Positive Tested Species Reactivity: Human, Primate
Depositors Notes: Inhibits binding of collagen to integrin alpha2beta1. This antibody doesn't appear to work for western blotting.
Antigen Molecular Weight: Predicted: 129 kDa; Apparent: 154 kDa under non-reducing conditions, 166 kDa under reducing conditions.
Human Protein Atlas:
Predicted Species Reactivity:  
Gene: ITGA2
Immunogen: Human platelets
Alternate Gene Names: CD49B, GPIA, BR, HPA-5, VLA-2
Alternate Antibody Name:
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped: Yes
Myeloma Strain: X63-Ag8.653
Epitope Location or Sequence: I domain of alpha2 (aa 173-259)
Uniprot ID: P17301 
Immunogen Sequence: Full length protein
Entrez Gene ID: 3673 
Additional Characterization:
Antibody Registry ID: AB_2617392 
Additional Information: 6F1 recognizes alpha2 in its native conformation associated to beta1 integrin.
Recommended Applications: ELISA, FACS, Function Blocking, Immunoprecipitation
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:
6F1 was deposited to the DSHB by Coller, B.S. (DSHB Hybridoma Product 6F1)
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. To ensure retention of antibody activity, we recommend aliquotting the product into two parts: 1) a volume of antibody stored at 4°C to be used within two weeks. 2) the remaining product diluted with an equal volume of molecular grade glycerol and stored at -20°C.
Usage Recommendations
While optimal Ig concentration for an application will vary, a good starting concentration for immunohistochemistry (IHC), immunofluorescence(IF) and staining is 2-5 µg/ml. For Western blots, the concentration is decreased by one order of magnitude (that is, 0.2-0.5 µg/ml).
All cell products contain the antimicrobial ProClin. Click here for additional information.

24 References

  • Initial Publication
  • IP References
  • ELISA References
  • FB References
  • FACS References
  • Epitope Map References
  • All References
  • Initial Publication
    IP References
    ELISA References
    FB References

    Collagen-platelet interactions: evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins.
    Steinberg MH
    Blood 74.1 (1989 Jul): 182-92.

    Thrombospondin-induced adhesion of human platelets.
    Kowalska MA
    The Journal of clinical investigation 87.4 (1991 Apr): 1387-94.

    Integrin alpha 2 I-domain is a binding site for collagens.
    Humphries MJ
    Journal of cell science 108 ( Pt 4). (1995 Apr): 1629-37.

    The integrin alpha 2 beta 1 (GPIa/IIa)-I-domain inhibits platelet-collagen interaction.
    Deckmyn H
    Thrombosis and haemostasis 77.5 (1997 May): 981-5.

    Contributions of the I and EF hand domains to the divalent cation-dependent collagen binding activity of the alpha2beta1 integrin.
    Santoro SA
    The Journal of biological chemistry 272.12 (1997 Mar 21): 7661-8.

    Effects of neuroblastoma tumor gangliosides on platelet adhesion to collagen.
    Valentino LA
    Clinical and experimental metastasis 15.1 (1997 Jan): 33-40.

    Adhesion and activation of human platelets induced by convulxin involve glycoprotein VI and integrin alpha2beta1.
    Bon C
    The Journal of biological chemistry 272.43 (1997 Oct 24): 27035-41.

    Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding.
    Santoro SA
    Cell adhesion and communication 5.4 (1998 Jun): 273-81.

    Simple collagen-like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces.
    Sixma JJ
    Blood 91.10 (1998 May 15): 3808-16.

    Functional analysis of a recombinant glycoprotein Ia/IIa (Integrin alpha(2)beta(1)) I domain that inhibits platelet adhesion to collagen and endothelial matrix under flow conditions.
    Cruz MA
    The Journal of biological chemistry 274.50 (1999 Dec 10): 35921-6.

    Studies of adhesion-dependent platelet activation: distinct roles for different participating receptors can be dissociated by proteolysis of collagen.
    Lassila R
    Arteriosclerosis, thrombosis, and vascular biology 19.12 (1999 Dec): 3033-43.

    Different role of platelet glycoprotein GP Ia/IIa in platelet contact and activation induced by type I and type III collagens.
    Fauvel-Lafève F
    Thrombosis research 98.5 (2000 Jun 1): 423-33.

    Involvement of activated integrin alpha2beta1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions.
    Jung SM
    Thrombosis and haemostasis 83.5 (2000 May): 769-76.

    Distinct roles of GPVI and integrin alpha(2)beta(1) in platelet shape change and aggregation induced by different collagens.
    Watson SP
    British journal of pharmacology 137.1 (2002 Sep): 107-17.

    Platelet receptor interplay regulates collagen-induced thrombus formation in flowing human blood.
    Heemskerk JW
    Blood 103.4 (2004 Feb 15): 1333-41.

    The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor alpha2beta1 to bind collagen: activation-dependent conformational change of the alpha2-I domain.
    López JA
    Blood 105.5 (2005 Mar 1): 1986-91.

    Human atheromatous plaques stimulate thrombus formation by activating platelet glycoprotein VI.
    Siess W
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology 19.8 (2005 Jun): 898-909.

    Use of synthetic peptides to locate novel integrin alpha2beta1-binding motifs in human collagen III.
    Farndale RW
    The Journal of biological chemistry 281.7 (2006 Feb 17): 3821-31.

    The leech product saratin is a potent inhibitor of platelet integrin alpha2beta1 and von Willebrand factor binding to collagen.
    McCarty OJ
    The FEBS journal 274.6 (2007 Mar): 1481-91.

    Structure-guided design of a high-affinity platelet integrin αIIbβ3 receptor antagonist that disrupts Mg²⁺ binding to the MIDAS.
    Coller BS
    Science translational medicine 4.125 (2012 Mar 14): 125ra32.

    FACS References
    Epitope Map References

    Identification of putative ligand binding sites within I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29)
    Takada Y
    The Journal of biological chemistry 269.13 (1994 Apr 1): 9659-63.

    All References

    Collagen-platelet interactions: evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins.
    Steinberg MH
    Blood 74.1 (1989 Jul): 182-92.

    Identification of putative ligand binding sites within I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29)
    Takada Y
    The Journal of biological chemistry 269.13 (1994 Apr 1): 9659-63.

    Contributions of the I and EF hand domains to the divalent cation-dependent collagen binding activity of the alpha2beta1 integrin.
    Santoro SA
    The Journal of biological chemistry 272.12 (1997 Mar 21): 7661-8.

    Mapping the collagen-binding site in the I domain of the glycoprotein Ia/IIa (integrin alpha(2)beta(1)).
    Cruz MA
    The Journal of biological chemistry 275.6 (2000 Feb 11): 4205-9.

    Thrombospondin-induced adhesion of human platelets.
    Kowalska MA
    The Journal of clinical investigation 87.4 (1991 Apr): 1387-94.

    Integrin alpha 2 I-domain is a binding site for collagens.
    Humphries MJ
    Journal of cell science 108 ( Pt 4). (1995 Apr): 1629-37.

    The integrin alpha 2 beta 1 (GPIa/IIa)-I-domain inhibits platelet-collagen interaction.
    Deckmyn H
    Thrombosis and haemostasis 77.5 (1997 May): 981-5.

    Effects of neuroblastoma tumor gangliosides on platelet adhesion to collagen.
    Valentino LA
    Clinical and experimental metastasis 15.1 (1997 Jan): 33-40.

    Adhesion and activation of human platelets induced by convulxin involve glycoprotein VI and integrin alpha2beta1.
    Bon C
    The Journal of biological chemistry 272.43 (1997 Oct 24): 27035-41.

    Binding of the alpha 2 integrin I domain to extracellular matrix ligands: structural and mechanistic differences between collagen and laminin binding.
    Santoro SA
    Cell adhesion and communication 5.4 (1998 Jun): 273-81.

    Simple collagen-like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces.
    Sixma JJ
    Blood 91.10 (1998 May 15): 3808-16.

    Functional analysis of a recombinant glycoprotein Ia/IIa (Integrin alpha(2)beta(1)) I domain that inhibits platelet adhesion to collagen and endothelial matrix under flow conditions.
    Cruz MA
    The Journal of biological chemistry 274.50 (1999 Dec 10): 35921-6.

    Studies of adhesion-dependent platelet activation: distinct roles for different participating receptors can be dissociated by proteolysis of collagen.
    Lassila R
    Arteriosclerosis, thrombosis, and vascular biology 19.12 (1999 Dec): 3033-43.

    Different role of platelet glycoprotein GP Ia/IIa in platelet contact and activation induced by type I and type III collagens.
    Fauvel-Lafève F
    Thrombosis research 98.5 (2000 Jun 1): 423-33.

    Involvement of activated integrin alpha2beta1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions.
    Jung SM
    Thrombosis and haemostasis 83.5 (2000 May): 769-76.

    Distinct roles of GPVI and integrin alpha(2)beta(1) in platelet shape change and aggregation induced by different collagens.
    Watson SP
    British journal of pharmacology 137.1 (2002 Sep): 107-17.

    Platelet receptor interplay regulates collagen-induced thrombus formation in flowing human blood.
    Heemskerk JW
    Blood 103.4 (2004 Feb 15): 1333-41.

    The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor alpha2beta1 to bind collagen: activation-dependent conformational change of the alpha2-I domain.
    López JA
    Blood 105.5 (2005 Mar 1): 1986-91.

    Human atheromatous plaques stimulate thrombus formation by activating platelet glycoprotein VI.
    Siess W
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology 19.8 (2005 Jun): 898-909.

    Use of synthetic peptides to locate novel integrin alpha2beta1-binding motifs in human collagen III.
    Farndale RW
    The Journal of biological chemistry 281.7 (2006 Feb 17): 3821-31.

    The leech product saratin is a potent inhibitor of platelet integrin alpha2beta1 and von Willebrand factor binding to collagen.
    McCarty OJ
    The FEBS journal 274.6 (2007 Mar): 1481-91.

    Structure-guided design of a high-affinity platelet integrin αIIbβ3 receptor antagonist that disrupts Mg²⁺ binding to the MIDAS.
    Coller BS
    Science translational medicine 4.125 (2012 Mar 14): 125ra32.

    A collagen-like peptide stimulates tyrosine phosphorylation of syk and phospholipase C gamma2 in platelets independent of the integrin alpha2beta1.
    Watson SP
    Blood 89.4 (1997 Feb 15): 1235-42.

    The metalloprotease, NN-PF3 from Naja naja venom inhibits platelet aggregation primarily by affecting α2β1 integrin.
    Kemparaju K
    Annals of hematology 90.5 (2011 May): 569-77.

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