Vaspin Active Protein | SERPINA12 active protein

Human Vaspin

Cat. Num. AAA691922

• Gene Names: SERPINA12; OL-64
• Reactivity: Human
• Purity: 98 % (SDS-PAGE, HPLC)
• Synonyms: Vaspin; Human Vaspin; Recombinant Human Vaspin; SERPINA12 active protein

• Host: E Coli
• Reactivity: Human
• Purity/Purification: 98 % (SDS-PAGE, HPLC)
• Form/Format: Lyophilized
• Sequence: MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAF YNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE K DLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKN FYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TV MLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIY QV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTF SRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDL T KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLV VKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK
• Sequence Length: 414

• Endotoxin Level: < 0.1 ng per ug of Vaspin
• Biological Activity: Data not available.

Related Product Information for SERPINA12 active protein

Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three beta-sheets, nine alpha-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal") serine-protease inhibitors, characterized by having more than 30% sequence homology with alpha1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is alpha1- antitrypsin. Vaspin exhibits 40.2% sequence identity with alpha-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-alpha. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.

Product Categories/Family for SERPINA12 active protein

Cytokines & Growth Factors

NCBI and Uniprot Product Information

• NCBI GI #: 27777657
• NCBI GeneID: 145264
• NCBI Accession #: NP_776249.1
• NCBI GenBank Nucleotide #: NM_173850.2
• UniProt Accession #: Q8IW75
• Molecular Weight: 22.2 kDa
• NCBI Official Full Name: serpin A12
• NCBI Official Synonym Full Names: serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12
• NCBI Official Symbol: SERPINA12
• NCBI Official Synonym Symbols: OL-64
• NCBI Protein Information: serpin A12; vaspin; visceral adipose-specific SERPIN; visceral adipose tissue-derived serine protease inhibitor; serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12
• UniProt Protein Name: Serpin A12
• Protein Family: Serpin
• UniProt Gene Name: SERPINA12
• UniProt Synonym Gene Names: Vaspin
• UniProt Entry Name: SPA12_HUMAN

Uniprot Description

Function: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. Ref.1

Subunit structure: Forms a stable complex with KLK7. Ref.4

Subcellular location: Secreted.

Tissue specificity: Expressed in visceral adipose tissues. Ref.1

Domain: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable

By similarity.

Sequence similarities: Belongs to the serpin family.