|Application ||WB, FC, E|
|Calculated MW||23858 Da|
|Antigen Region||19-45 aa|
|Other Names||Regulator of G-protein signaling 1, RGS1, B-cell activation protein BL34, Early response protein 1R20, RGS1, 1R20, BL34, IER1|
|Target/Specificity||This RGS1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 19-45 amino acids from the N-terminal region of human RGS1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RGS1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||1R20, BL34, IER1|
|Function||Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. This protein may be involved in the regulation of B-cell activation and proliferation.|
|Tissue Location||B-cell specific. Expression is relatively low in B-cells and chronic lymphocytic leukemia B-cells; however, in other types of malignant B-cell such as non-Hodgkin lymphoma and hairy cell leukemia, expression is constitutively high|
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Provided below are standard protocols that you may find useful for product applications.
RGS1 is a member of the regulator of G-protein signalling family. This protein is located on the cytosolic side of the plasma membrane and contains a conserved, 120 amino acid motif called the RGS domain. The protein attenuates the signalling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal.
Bowman,E.P., et.al., J. Biol. Chem. 273 (43), 28040-28048 (1998)
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