The Anti-CD43 Recombinant Rabbit Monoclonal Antibody (HDAB0202) is a valuable tool for researchers studying CD43, a glycoprotein involved in immune response regulation. This antibody, produced in rabbits, shows high specificity and reactivity with human samples, making it ideal for Western blot applications. By binding to the CD43 protein, this antibody enables the detection and analysis of CD43 expression in various cell types.CD43, also known as leukosialin, plays a crucial role in immune cell adhesion and activation. Its involvement in immune regulation makes it a promising target for research in immunology and cancer biology.
Understanding the function of CD43 can provide insights into immune system dysregulation in diseases such as cancer, autoimmune disorders, and inflammatory conditions.Overall, the Anti-CD43 Recombinant Rabbit Monoclonal Antibody (HDAB0202) offers researchers a reliable tool for studying CD43 expression and its role in immune response modulation, making it a valuable asset in the field of immunology and cancer research.
SKU:
HDAB0202
Size:
100 µg
Clonality:
Monoclonal
Clone:
DM211
Synonyms:
CD43, GALGP, GPL115, LSN
Applications:
ELISA, Flow Cyt
Recommended Dilution:
ELISA 1:5000-10000; Flow Cyt 1:100
Host Species:
Rabbit
Isotype:
Rabbit IgG
Reactivity:
Human
Purification Method:
Purified from cell culture supernatant by affinity chromatography
Formulation:
Powder
Buffer:
1XPBS
Storage:
Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing).Lyophilized antibodies are shipped at ambient temperature.
Usage:
Research use only
Background:
This gene encodes a highly sialylated glycoprotein that functions in antigen-specific activation of T cells, and is found on the surface of thymocytes, T lymphocytes, monocytes, granulocytes, and some B lymphocytes. It contains a mucin-like extracellular domain, a transmembrane region and a carboxy-terminal intracellular region. The extracellular domain has a high proportion of serine and threonine residues, allowing extensive O-glycosylation, and has one potential N-glycosylation site, while the carboxy-terminal region has potential phosphorylation sites that may mediate transduction of activation signals. Different glycoforms of this protein have been described. In stimulated immune cells, proteolytic cleavage of the extracellular domain occurs in some cell types, releasing a soluble extracellular fragment. Defects in expression of this gene are associated with Wiskott-Aldrich syndrome. [provided by RefSeq, Sep 2017]
