DescriptionCD28 homolog (CD28H), also called TMIG2 and IGPR-1, is a 55kDa glycosylated transmembrane protein that shares approximately 10% amino acid (aa) sequence identity with CD28, CTLA-4, ICOS, and PD-1. CD28H is composed of a single extracellular immunoglobulin variable-like domain (IgV) (aa 23-109), a transmembrane domain (aa 151-171), and a long cytoplasmic domain (aa172-282). CD28H is constitutively expressed on naive T and NK cells. Similar to the interaction of B7 with CD28, the interaction of CD28H with B7-H7 activates the Akt-dependent signaling cascade and promotes the proliferation and activation of newly generated peripheral effector and memory T cells (1, 2). CD28H is additionally expressed in the skin and epithelium lining the lung, airway, mammary gland, and gastrointestinal tract (3). It regulates cellular morphology, focal adhesion contact formation, and cell migration (3, 4). CD28H also participates in angiogenesis in vitro (3). CD28H interacts with multiple cytoskeletal proteins including Actin, Paxillin, SPIN90, CACNB2, and BPAG1. Interactions between the cytoplasmic proline-rich domain of CD28H and SPIN90 modulate the activity of CD28H in both angiogenesis and cell adhesion (3, 5).
|CyTOF, Flow Cytometry, Immunohistochemistry|
|Protein A or G purified from hybridoma culture supernatant|
|Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 μm filtered solution in PBS. with No Preservative|
|Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 6 months, -20 to -70 degreesC under sterile conditions after reconstitution.|
We continue to work to improve your shopping experience and your feedback regarding this content is very important to us. Please use the form below to provide feedback related to the content on this product.
Your feedback has been submitted. Fisher Scientific is always working to improve our content for you. We appreciate your feedback.Ok