Recombinant Human SerpinI2 Protein (His Tag)

Name :
Recombinant Human SerpinI2 Protein (His Tag)

Biological Activity :

Background :
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some 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. Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein that belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption.

Biological Activity :
Testing in progress

Expression Host :
Human

Source :
HEK293 Cells

Tag :

Protein Accession No. :
NP_006208.1

NCBI Gene ID :

Synonyms :

Synonyms :
serpin peptidase inhibitor, clade I (pancpin), member 2

Amino Acid Sequence :

Molecular Weight :
The recombinant human SERPINI2 consists of 398 amino acids and predictes a molecular mass of 45.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhSERPINI2 is approximately 45-55 kDa due to glycosylation.

Purity :
> 90 % as determined by SDS-PAGE

State of Matter :

Product Concentration :

Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method

Protein Construction :
A DNA sequence encoding the human SERPINI2 (NP_006208.1) (Met 1-Leu 405) was expressed, with a polyhistidine tag at the C-terminus.

Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :
MEPI Protein, Human; PANCPIN Protein, Human; PI14 Protein, Human; Serpin I2 Protein, Human; TSA2004 Protein, Human SerpinI2 背景信息 Serpins are the largest and most diverse family of serine protease inhibitors which are involved in some 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. Serpin-I2, also known as myoepithelium-derived serine protease inhibitor, Pancreas-specific protein TSA24, Peptidase inhibitor 14, PI14, SERPINI2 and MEPI, is a secreted protein that belongs to the serpin family. It is expressed in pancreas and adipose tissues. SERPINI2 deficiency directly results in the acinar cell apoptosis and malabsorption.

References & Citations :
Riewald M. et al., 1995, J. Biol. Chem. 270: 26754-7. Forsyth, S. et al., 2003, Genomics 81: 336-45. Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-97. Loftus,S.K. et al., 2005, PLoS Genet. 1 (3):e38. Steenbakkers PJ. et al., 2008, Mycol. Res. 112 (Pt 8): 999-1006. Przygodzka, P. et al., 2010, BMC Cell Biol. 11: 30.

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