6F1

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SKU: 6F1-s

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DSHB Data Sheet

Catalog Fields

Clone ID/Product Name: 6F1
Available to For-Profits: Yes
Alternate Antibody Name:
Gene Symbol: ITGA2
Ab Isotype: MIgG1
Gene Name:
Antibody Registry ID: AB_2617392 
Uniprot ID: P17301 
RRID:  
Entrez Gene ID: 3673 
Clonality: Monoclonal
Immunogen: Human platelets
Clone:
Immunogen Sequence: Full length protein
Myeloma Strain: X63-Ag8.653
Epitope Mapped: Yes
Antigen Name: integrin alpha-2 (CD49B), human
Epitope Location or Sequence: I domain of alpha2 (aa 173-259)
Alternate Antigen Name:
Deposit Date: 3/3/2012
Antigen Molecular Weight: Predicted: 129 kDa; Apparent: 154 kDa under non-reducing conditions, 166 kDa under reducing conditions.
Depositor: Coller, B.S.
Antigen Sequence:
Depositor Institution: Rockefeller University
Antigen Species: Human
Depositor Notes: Inhibits binding of collagen to integrin alpha2beta1. This antibody doesn't appear to work for western blotting.
Host Species: mouse
Hybridoma Cells Available (Non-Profit): No
Confirmed Species Reactivity: Human, Primate
Additional Information: 6F1 recognizes alpha2 in its native conformation associated to beta1 integrin.
Predicted Species Reactivity:  
Human Protein Atlas:  
Additional Characterization:  
Recommended Applications: ELISA, FACS, Function Blocking, Immunoprecipitation
All cell products contain the antimicrobial ProClin. Click here for additional information.
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. 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
The optimal Ig concentration for an application varies by species and antibody affinity. For each product, the antibody titer must be optimized for every application by the end user laboratory. A good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) when using mouse Ig is 2-5 ug/ml. For western blots, the recommended concentration range of mouse Ig 0.2-0.5 ug/ml. In general, rabbit antibodies demonstrate greater affinity and are used at a magnitude lower Ig concentration for initial testing. The recommended concentrations for rabbit Ig are 0.2-0.5 ug/ml (IF, IHC and ICC) and 20-50 ng/ml (WB).

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 & 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 & 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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