|Application ||WB, E|
|Other Accession||NP_848537, 41281905|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||75953 Da|
|Application Notes||KINDLIN3 antibody can be used for detection of KINDLIN3 by Western blot at 1 and 2 µg/mL.|
|Reconstitution & Storage||KINDLIN3 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||KINDLIN3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||KIND3, MIG2B, URP2|
|Function||Plays a central role in cell adhesion in hematopoietic cells (PubMed:19234463, PubMed:26359933). Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells (PubMed:19234460). Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).|
|Cellular Location||Cell projection, podosome. Note=Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells.|
|Tissue Location||Highly expressed in lymph node. Expressed in thymus, spleen and leukocytes. Weakly expressed in placenta, small intestine, stomach, testis and lung. Overexpressed in B-cell malignancies.|
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Provided below are standard protocols that you may find useful for product applications.
KINDLIN3 Antibody: The three KINDLINs are a novel family of focal adhesion proteins, localizing to integrin adhesion sites. The KINDLIN proteins are composed of a centrally located FERM domain interrupted by a pleckstrin homology (PH) domain. KINDLIN1 and KINDLIN2 have been shown to play an essential role in integrin-mediated adhesion and spreading. In contrast to the widely expressed KINDLIN1 and KINDLIN2, KINDLIN3 is restricted to hematopoietic cells and is particularly abundant in megakaryocytes and platelets. Several reports describe a transcriptional misregulation of KINDLINs in various types of cancer. A recent study demonstrates that KINDLIN3 is essential for platelet integrin activation and subsequent integrin outside-in signaling, suggesting it may serve as a potential target for the design of therapeutics aimed at specifically disrupting integrin activation in platelets and leukocytes.
Ussar S, Wang HV, Linder S, et al. The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res.2006; 312:3142-51.
Weinstein EJ, Bourner M, Head R, et al. URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas. Biochim. Biophys. Acta2003; 1637:207-16.
Boyd RS, Adam PJ, Patel S, et al. Proteomic analysis of the cell-surface membrane in chronic lymphocytic leukemia: identification of two novel proteins, BCNP1 and MIG2B. Leukemia2003; 17:1605-12.
Mory A, Feigelson SW, Yarali N, et al. Kindlin-3: a new gene involved in the pathogenesis of LAD-III. Blood2008; 112:2591.
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