The GELE Antibody (PAC050726) is a highly specific polyclonal antibody designed for research involving the CD300A protein. CD300A is a cell surface molecule known for its role in immune regulation, particularly in inhibiting immune responses. The antibody, raised and purified in rabbits, is highly reactive with human samples and is validated for use in Western blot applications. By binding to the CD300A protein, this antibody enables the detection and analysis of CD300A in various cell types, making it an ideal tool for studies in immunology and cancer research. CD300A, also known as an immune inhibitory receptor, plays a crucial role in immune homeostasis by regulating inflammation and inhibiting allergic reactions.
Its significance in immune response modulation makes it a valuable target for research into diseases like cancer, autoimmune disorders, and chronic inflammatory conditions.Understanding the activity of CD300A is essential for developing therapies that harness or modulate immune function in these contexts. The GELE Antibody provides researchers with a reliable tool for studying the function and expression of CD300A, contributing to advancements in immunology and the development of potential treatments for immune-related diseases.
Antibody Name:
gelE Antibody (PACO50726)
Antibody SKU:
PACO50726
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:5000
Species Reactivity:
Enterococcus faecalis
Immunogen:
Recombinant Enterococcus faecalis Gelatinase protein (193-510AA)
Western Blot. Positive WB detected in Recombinant protein. All lanes: gelE antibody at 2µg/ml. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. predicted band size: 51 kDa. observed band size: 51 kDa..
Background:
Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe- |-Phe-25 bond in the insulin B-chain, followed by the 5-His- |-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser- |-Leu-6 and 16-His- |-Leu-17 bonds. Hydrolyzes the α chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin.
Synonyms:
Gelatinase (EC 3.4.24.30) (Coccolysin), gelE
UniProt Protein Function:
Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin.
