|Application ||WB, E|
|Calculated MW||77437 Da|
|Antigen Region||268-297 aa|
|Other Names||Fermitin family homolog 1, Kindlerin, Kindlin syndrome protein, Kindlin-1, Unc-112-related protein 1, FERMT1, C20orf42, KIND1, URP1|
|Target/Specificity||This FERMT1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 268-297 amino acids from the Central region of human FERMT1.|
|Precautions||FERMT1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||C20orf42, KIND1, URP1|
|Function||Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression.|
|Cellular Location||Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Constituent of focal adhesions. Localized at the basal aspect of skin keratinocytes, close to the cell membrane. Colocalizes with filamentous actin Upon TGFB1 treatment, it localizes to membrane ruffles|
|Tissue Location||Expressed in brain, skeletal muscle, kidney, colon, adrenal gland, prostate, and placenta. Weakly or not expressed in heart, thymus, spleen, liver, small intestine, bone marrow, lung and peripheral blood leukocytes. Overexpressed in some colon and lung tumors. In skin, it is localized within the epidermis and particularly in basal keratocytes. Not detected in epidermal melanocytes and dermal fibroblasts|
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Provided below are standard protocols that you may find useful for product applications.
FERMT1 is a member of the fermitin family, and contains a FERM domain and a pleckstrin homology domain. This protein is involved in integrin signaling and linkage of the actin cytoskeleton to the extracellular matrix.
Goult B.T., et.al., J. Mol. Biol. 394:944-956(2009).
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