KLK1 Human, His

Kallikrein-1 Human Recombinant, His Tag
Cat. No.
BT3004
Source
Escherichia Coli.
Synonyms
KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek'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

Kallikrein-1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (25-262) and having a molecular mass of 28.7kDa.
KLK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Kallikreins are a family of serine protease enzymes with diverse physiological roles. They have been linked to cancer development and show promise as potential biomarkers for the disease. KLK1 is a member of the kallikrein subfamily, consisting of fifteen members clustered on chromosome 19. A key function of KLK1 is the release of the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen, a function conserved across species. Also known as Kallidinogenase, Kininogenase, or Kininogenin, human Kallikrein-1 is an active enzyme found in saliva, pancreatic juices, and urine. It catalyzes the breakdown of bradykininogen to bradykinin. Human and porcine-derived Kallikrein-1 have a history of medicinal use, primarily for mild to moderate hypertension and treating blockages in the brain and surrounding blood vessels. KLK1 exhibits both trypsin- and chymotrypsin-like activities, showing a preference for Tyr/Arg at the P1 site, Ser/Arg at P1', and Phe/Leu at P2. Studies have shown a significant association between rs5517 in the KLK1 gene and hypertension in a Chinese Han population. KLK1 expression, observed to be de novo in endothelial cells, plays a role in relaxing human umbilical veins. The K allele of the KLK1 promoter and the TT genotype of TGF-beta1, along with KLK1 -130 GN and -128 G-C, have been identified as genetic susceptibility factors for progressive renal decline in Taiwanese children with primary vesicoureteric reflux. Interestingly, KLK1 induction in carotid arteriosclerosis does not activate the kallikrein-kinins pathway. Transgenic rats overexpressing KLK1 exhibit impaired renal response to acute volume expansion. Endothelial cells synthesize and release active KLK1, which plays a crucial role in maintaining circulatory homeostasis. KLK1 also participates in epidermal desquamation by cleaving desmoglein 1, a process regulated by the lympho-epithelial Kazal-type-related inhibitor (LEKTI).
Description
Recombinant human Kallikrein-1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 259 amino acids (residues 25-262) and has a molecular weight of 28.7kDa. The KLK1 protein includes a 21 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The KLK1 solution is provided at a concentration of 0.25mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 2-4 weeks), store the vial at 4°C. For extended storage, freeze the product at -20°C. To enhance long-term stability, consider adding a carrier protein like HSA or BSA (0.1%). Minimize freeze-thaw cycles to maintain product integrity.
Purity
The purity of KLK1 is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms
KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIVGGWECEQ HSQPWQAALY HFSTFQCGGI LVHRQWVLTA AHCISDNYQL WLGRHNLFDD ENTAQFVHVS ESFPHPGFNM SLLENHTRQA DEDYSHDLML LRLTEPADTI TDAVKVVELP TQEPEVGSTC LASGWGSIEP ENFSFPDDLQ CVDLKILPND ECKKVHVQKV TDFMLCVGHL EGGKDTCVGD SGGPLMCDGV LQGVTSWGYV PCGTPNKPSV AVRVLSYVKW IEDTIAENS.

Product Science Overview

Gene and Protein Structure

The KLK1 gene is located on chromosome 19 and is one of fifteen kallikrein subfamily members clustered in this region . The protein encoded by this gene is functionally conserved and is known for its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen .

Recombinant Expression

The Human Recombinant Kallikrein-1 (His Tag) is produced using an expression system in HEK293 cells . This recombinant protein includes a C-terminal His-tag, which facilitates its purification and detection. The amino acid sequence of this recombinant protein corresponds to the human KLK1 precursor, spanning from Met1 to Ser262 .

Functional Characteristics

Kallikrein-1 is involved in the proteolysis of bradykininogen to bradykinin, a peptide that plays a crucial role in various physiological processes, including blood pressure regulation, inflammation, and pain . The recombinant form of this protein is often used in research to study these processes and to explore its potential as a biomarker for diseases .

Applications and Storage

The recombinant KLK1 protein is used in various functional assays to study its enzymatic activity. It is typically lyophilized and stored at -20°C to maintain its stability . The protein is reconstituted in sterile water to prepare a stock solution for experimental use .

Clinical and Research Implications

Growing evidence suggests that many kallikreins, including KLK1, are implicated in carcinogenesis and may serve as novel biomarkers for cancer and other diseases . The ability to produce recombinant forms of these proteins allows researchers to study their functions in detail and to develop potential therapeutic applications.

In summary, Kallikrein-1 (Human Recombinant, His Tag) is a valuable tool in biomedical research, providing insights into the physiological roles of kallikreins and their potential implications in disease.

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