CBL1346Z-I
Anti-mouse Integrin alphaV Antibody, clone RMV-7 (Preservative free)
clone RMV-7, from rat
别名:
Integrin alpha-V, Vitronectin receptor subunit alpha, CD51, 1.Integrin alpha-V heavy chain2.Integrin alpha-V light chain, Integrin alphaV
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关于此项目
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
RMV-7, monoclonal
Application:
FACS, IP, WB
Citations:
3
biological source
rat
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
RMV-7, monoclonal
species reactivity
mouse
technique(s)
flow cytometry: suitable, immunoprecipitation (IP): suitable, western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Quality Level
Gene Information
mouse ... Itgav(16410)
General description
Integrin alphaV, also known as CD51, a member of the integrin family, is a 140 kD protein expressed on activated T cells, polymorphonuclear granulocytes, blastocysts, and osteoclasts. Integrin alphaV forms heterodimers by association with integrins beta1, beta3, beta5 or beta6, these complexes then act as receptors for multiple extracellular matrix proteins (ECM). The alphaV integrins have varied functions in development, stimulation/activation and homeostasis. The primary ligands for Integrin alphaV complexes are fibronectin, fibrinogen, vitronectin, thrombspondin, von Willebrand factor, and CD31.
~140 kDa observed. The calculated molecular weight is 115 kDa, however Integrin alphaV has been shown as a ~140 kDa band in western blots (Takahashi, K. et al., (1990). J. Immunol. 145:4371.).
Immunogen
BALB/c mouse IL-2–activated killer (LAK) cells
Application
This Anti-mouse Integrin alphaV Antibody, clone RMV-7 (Preservative free) is validated for use in Western Blotting, Immunoprecipitation, Flow Cytometry for the detection of mouse Integrin alphaV.
Western Blot Analysis: A representative lot was used by an independent laboratory in LAK cell lysate. (Takahashi, K. et al., (1990). J. Immunol. 145:4371.)
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in LAK cell lysate. (Takahashi, K. et al., (1990). J. Immunol. 145:4371.)
Blocking Assay: Adhesion and LAK cell cytotoxicity was shown using a representative lot (Takahashi, K. et al., (1990). J. Immunol. 145:4371.)
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in LAK cell lysate. (Takahashi, K. et al., (1990). J. Immunol. 145:4371.)
Blocking Assay: Adhesion and LAK cell cytotoxicity was shown using a representative lot (Takahashi, K. et al., (1990). J. Immunol. 145:4371.)
Biochem/physiol Actions
Specifically recognizes Integrin alphaV, also known as CD51 or vitronectin receptor. This antibody has been reported to block binding of Integrin alphaV to vitronectin, fibronectin, fibrinogen, and CD31 in some cell types, as well as, blocking LAK cell cytotoxicity.
Physical form
Format: Purified
Analysis Note
Control
Murine 3T3-L1 cells
Murine 3T3-L1 cells
Evaluated by Flow Cytometry in murine 3T3-L1 cells.
Flow Cytometry Analysis: 0.2 µg of this antibody detected Integrin alphaV in murine 3T3-L1 cells .
Flow Cytometry Analysis: 0.2 µg of this antibody detected Integrin alphaV in murine 3T3-L1 cells .
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: CBL1346Z
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存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
K Takahashi et al.
Journal of immunology (Baltimore, Md. : 1950), 145(12), 4371-4379 (1990-12-15)
CD2 and lymphocyte function-associated antigen (LFA)-1 are well known as T cell adhesion molecules involved in killer-target cell interactions. However, our recent study revealed that molecule(s) other than CD2 and LFA-1 might be involved in the lymphokine-activated killer (LAK) cell
Yongen Chang et al.
Journal of the American Society of Nephrology : JASN, 28(7), 1998-2005 (2017-02-22)
Activated fibroblasts are deemed the main executors of organ fibrosis. However, regulation of the pathologic functions of these cells in vivo is poorly understood. PDGF receptor β (PDGFRβ) is highly expressed in activated pericytes, a main source of fibroblasts. Studies
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