SERPINA4 Human

Kallistatin Human Recombinant
Cat. No.
BT23277
Source
HEK 293.
Synonyms
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

SERPINA4 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Gln21-Pro427) containing a total of 417 amino acids, having a calculated molecular mass of 47.7kDa and fused to a 10 aa His tag at C-Terminus.

Product Specs

Introduction
Kallistatin, also known as SERPINA4, acts as an inhibitor of tissue kallikrein, effectively hindering both its amidolytic and kininogenase functions in humans. This inhibitory action is achieved through the formation of a highly stable, equimolar complex between kallistatin and the enzyme. The complex is resistant to heat and SDS. Notably, the interaction leads to the cleavage of kallistatin at a specific reactive site by tissue kallikrein, resulting in the generation of a small C-terminal fragment.
Description
Recombinant human SERPINA4, expressed in HEK cells, is a single-chain polypeptide that has undergone glycosylation. It encompasses amino acids Gln21 to Pro427, resulting in a protein with 417 amino acids. With a predicted molecular weight of 47.7 kDa, this recombinant SERPINA4 is further modified by the addition of a 10-amino acid histidine tag at its C-terminus.
Physical Appearance
White powder, lyophilized and sterile-filtered.
Formulation
The SERPINA4 protein underwent a 0.4 μm filtration process before being lyophilized. The lyophilization was performed from a solution containing 0.5 mg/ml SERPINA4 in phosphate-buffered saline (pH 7.4) supplemented with 5% (w/v) Trehalose.
Solubility

To generate a working stock solution, it is advisable to add deionized water to the lyophilized pellet, aiming for a concentration of roughly 0.5 mg/ml. Allow adequate time for the pellet to completely dissolve. It's essential to note that SERPINA4 is not sterile in its lyophilized form. Prior to using it for cell culture applications, ensure sterility by filtering the reconstituted protein through an appropriate sterile filter.

Stability
For long-term storage, maintain the lyophilized SERPINA4 protein at -20°C. After reconstitution, it's recommended to aliquot the protein solution to minimize freeze-thaw cycles. The reconstituted protein demonstrates stability at 4°C for a limited duration; storage at this temperature for two weeks has shown no discernible changes in the protein.
Purity
Purity levels exceed 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
Source
HEK 293.
Amino Acid Sequence
QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK VVDPTKPHHH HHHHHHH.

Product Science Overview

Structure and Function

Kallistatin consists of three folded β segments and eight helical structures, containing two functional domains: an active site and a heparin-binding site . It functions primarily as an inhibitor of tissue kallikrein, a serine protease involved in the kinin-kallikrein system, which regulates blood pressure, inflammation, and coagulation .

Biological Roles
  1. Inhibition of Tissue Kallikrein: Kallistatin specifically inhibits tissue kallikrein, thereby regulating the production of kinins, which are peptides that influence blood pressure and inflammation .
  2. Anti-Angiogenic and Anti-Tumor Properties: Kallistatin has been shown to inhibit angiogenesis (the formation of new blood vessels) and tumor growth, making it a potential therapeutic target for cancer treatment .
  3. Vascular Remodeling: Kallistatin plays a role in vascular remodeling, which is crucial for maintaining vascular homeostasis and function .
Expression and Tissue Distribution

Kallistatin is expressed in various tissues, including the liver, pancreas, gallbladder, epididymis, stomach, and muscle . Its widespread expression suggests that it has multiple physiological roles across different organ systems.

Recombinant Kallistatin

Recombinant human kallistatin is produced using advanced biotechnological methods. It is typically expressed in a mouse myeloma cell line (NS0) and purified to high levels of purity . The recombinant form retains the functional properties of the native protein, making it useful for research and potential therapeutic applications.

Clinical Implications

Given its role in inhibiting angiogenesis and tumor growth, kallistatin is being explored for its therapeutic potential in cancer treatment. Additionally, its ability to regulate blood pressure and inflammation positions it as a candidate for treating cardiovascular diseases and inflammatory conditions .

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