SERPINI1 Human
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.
Description
SERPINI1 is purified by proprietary chromatographic techniques.
Product Specs
MTGATFPEEA IADLSVNMYN RLRATGEDEN ILFSPLSIAL AMGMMELGAQ
GSTQKEIRHS MGYDSLKNGE EFSFLKEFSN MVTAKESQYV MKIANSLFVQ
NGFHVNEEFL QMMKKYFNAA VNHVDFSQNV AVANYINKWV ENNTNNLVKD
LVSPRDFDAA TYLALINAVY FKGNWKSQFR PENTRTFSFT KDDESEVQIP
MMYQQGEFYY GEFSDGSNEA GGIYQVLEIP YEGDEISMML VLSRQEVPLA
TLEPLVKAQL VEEWANSVKK QKVEVYLPRF TVEQEIDLKD VLKALGITEI
FIKDANLTGL SDNKEIFLSK AIHKSFLEVN EEGSEAAAVS GMIAISRMAV
LYPQVIVDHP FFFLIRNRRT GTILFMGRVM HPETMNTSGH DFEEL.
Product Science Overview
Serpin Peptidase Inhibitor, Clade I Member 1, also known as SERPINI1, is a member of the serpin (serine protease inhibitor) superfamily. This family of proteins plays a crucial role in regulating various physiological processes by inhibiting serine proteases. SERPINI1 is particularly significant due to its involvement in neuroprotection and its association with certain neurological disorders.
SERPINI1 belongs to the clade I of the serpin family, which is characterized by its unique structural features. The protein typically consists of three beta-sheets, nine alpha-helices, and a central reactive center loop (RCL). The RCL acts as a pseudo-substrate for target proteases, leading to the formation of a stable complex that inhibits the protease activity.
SERPINI1 is primarily expressed in the nervous system, particularly in the brain. It is known for its neuroprotective properties, which are crucial for maintaining neuronal health and function. The protein inhibits tissue plasminogen activator (tPA), a serine protease involved in the breakdown of blood clots. By inhibiting tPA, SERPINI1 helps prevent excessive proteolytic activity that can lead to neuronal damage.
The expression of SERPINI1 is predominantly observed in the brain, with high levels in regions such as the cerebral cortex, hippocampus, and cerebellum. This distribution pattern suggests its significant role in central nervous system (CNS) functions. Additionally, SERPINI1 expression can be influenced by various factors, including developmental stages and pathological conditions.
The primary function of SERPINI1 is to inhibit tPA, thereby regulating extracellular proteolysis in the CNS. This inhibition is essential for maintaining the integrity of the blood-brain barrier and preventing neurodegeneration. SERPINI1 also plays a role in synaptic plasticity, learning, and memory by modulating the extracellular matrix and influencing neuronal connectivity.
SERPINI1 exerts its inhibitory effect through a “suicidal” mechanism, where the RCL of the serpin interacts with the active site of the target protease. This interaction leads to a conformational change in SERPINI1, trapping the protease in a stable complex and rendering it inactive. This irreversible inhibition is a hallmark of serpin family members.
The expression and activity of SERPINI1 are tightly regulated at multiple levels. Transcriptional regulation involves various factors that respond to developmental cues and environmental stimuli. Post-translational modifications, such as glycosylation, also play a role in modulating the stability and activity of SERPINI1. Additionally, interactions with other proteins and cellular components can influence its inhibitory function.
Mutations in the SERPINI1 gene are associated with a rare neurological disorder known as familial encephalopathy with neuroserpin inclusion bodies (FENIB). This condition is characterized by the accumulation of mutant SERPINI1 in neurons, leading to the formation of inclusion bodies and progressive neurodegeneration. Understanding the molecular mechanisms underlying SERPINI1 function and regulation is crucial for developing therapeutic strategies for FENIB and other related disorders.
