serpin family

Serpin B6 belongs to the serpin family. Serpin B6 localizes to the cytoplasm. Serpin B6 is expressed in many tissues, abundantly by mast cells in different tissues and mastocytoma lesions. Serpin B6 may be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. In addition, Serpin B6 may play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss.

Expression system: E. coli
Length: 21-414, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 43-417, Partial
Activity: Not Tested

As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. Serpin G1 is a serine protease inhibitor protein. It is the largest member among the serpin class of proteins. Remarkably, Serpin G1 has a 2-domain structure, unlike most family members. The C-terminal serpin domain is similar to other serpins, and this part of Serpin G1 provides the inhibitory activity. The N-terminal domain is not essential for Serpin G1 to inhibit proteinases and has no similarity to other proteins. The main function of Serpin G1 is the inhibition of the complement system to prevent spontaneous activation. Serpin G1 is an acute phase protein and circulates in blood at levels of around 0.25g L, whose levels rise 2-fold during inflammation. Although named after its complement inhibitory activity, Serpin G1 also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Most notably, Serpin G1 play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. It is also the most important physiological inhibitor of fXIIa, chymotrypsin and plasma kallikrein.

Plasminogen activator inhibitor-1 (serpin E1) is a serine protease inhibitor which belongs to the serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3 TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.

Expression system: HEK293 Cells
Length: 20-397, Full Length of Mature Protein of Isoform 2
Activity: Not Tested

Expression system: HEK293 Cells
Length: 21-427, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 19-418, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-504, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 25-413, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-425, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 22-444, Full Length of Mature Protein
Activity: Not Tested

PEDF Protein, Human, Recombinant is expressed in E. coli. The accession number is P36955.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified. Mouse Serpin A11, also known as SERPINA11, is a member of the serpin family.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.Mouse SerpinB8, also known as Cytoplasmic antiproteinase 2, Peptidase inhibitor 8, SerpinB8, PI-8, SERPINB8 and CAP2, is a member of the Serpin superfamily. SERPINB8 was broadly expressed. In normal neuroendocrine tissues, strongest SerpinB8 expression was detected in islets of Langerhans of the pancreas. Moderate SerpinB8 expression was observed in neuroendocrine cells of the thyroid, adrenal cortex, colon, and pituitary gland. In the pancreas, SerpinB8 is specifically expressed by insulin-producing beta cells, and can be used as an additional diagnostic immunohistochemical marker. Mouse SerpinB8 distribution alters during kidney regeneration, possibly to control a prohormone convertase involved in inflammation or tissue repair.

Expression system: Baculovirus Insect Cells
Length: 1-397, Full Length
Activity: Not Tested

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified.Mouse SerpinB3, also known as Squamous cell carcinoma antigen 1, SCCA-1, SERPINB3, SCCA and SCCA1, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB3 may act as a protease inhibitor to modulate the host immune response against tumor cells. Mouse SerpinB3a and SerpinB3b, but not Serpinb3c, are functional, inhibiting both serine and cysteine proteinases with different inhibitory profiles due to the difference of two amino acids in their reactive site loops. SerpinB3a is ubiquitously expressed in most tissues, whereas expression of SerpinB3b is limited to keratinocytes. SerpinB3a and SerpinB3b may play different roles by inhibiting intrinsic or extrinsic proteinases with different expression distributions and different inhibitory profiles.

Expression system: Baculovirus Insect Cells
Length: 1-415, Full Length
Activity: ELISA

Expression system: Baculovirus Insect Cells
Length: 1-423, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-405, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-448, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-414, Full Length
Activity: Enzyme activity

Expression system: Baculovirus Insect Cells
Length: 2-376, Partial
Activity: Not Tested

SerpinB6, also known as Cytoplasmic antiproteinase, Peptidase inhibitor 6, Placental thrombin inhibitor, SERPINB6 and PI-6, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB6 PI-6 is an inhibitor of cathepsin G, kallikrein-8 and thrombin. It may play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss. SerpinB6 PI-6 is expressed in keratinocytes (at protein level). It is also found in placenta, cardiac muscle, lung, liver, kidney and pancreas. SerpinB6 PI-6 is expressed in the inner ear hair cells. It's expressed abundantly by normal mast cells in different tissues and by mast cells in mastocytoma lesions. SerpinB6 PI-6 may be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. Defects in SerpinB6 are the cause of deafness autosomal recessive type 91 which is a form of non-syndromic deafness characterized by progressive and age-dependent sensorineural hearing loss. Vestibular function is normal.