KLK15 Human, sf9

Kallikrein-15 Human Recombinant, sf9
Cat. No.
BT3787
Source
Sf9, Baculovirus cells.
Synonyms

Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-,  EC 3.4.21, HSRNASPH, ACO.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 80.0% 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

KLK15 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 249 amino acids (17-256a.a.) and having a molecular mass of 27.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
KLK15 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Kallikrein-15 (KLK15), a member of the kallikrein subfamily found on chromosome 19, exhibits diverse transcript variants due to alternative splicing and multiple polyadenylation sites, leading to various isoforms. KLK15's overexpression in prostate cancer marks its potential as a diagnostic or prognostic indicator for the disease.
Description
Recombinantly produced in Sf9 Baculovirus cells, KLK15 Human Recombinant is a single, glycosylated polypeptide chain consisting of 249 amino acids (17-256a.a.). With a molecular mass of 27.4kDa, it appears on SDS-PAGE around 28-40kDa. The protein features a 6 amino acids His tag at the C-terminus and undergoes purification through proprietary chromatographic techniques.
Physical Appearance
The product is a sterile-filtered solution, colorless in appearance.
Formulation
The KLK15 protein solution is provided at a concentration of 0.25mg/ml, dissolved in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product should be kept at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. To maintain product integrity, avoid repeated freeze-thaw cycles.
Purity
The purity of KLK15 Human Recombinant is determined to be greater than 80.0% based on SDS-PAGE analysis.
Synonyms

Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-,  EC 3.4.21, HSRNASPH, ACO.

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

ADPQDGDKLL EGDECAPHSQ PWQVALYERG RFNCGASLIS PHWVLSAAHC QSRFMRVRLG EHNLRKRDGP EQLRTTSRVI PHPRYEARSH RNDIMLLRLV QPARLNPQVR PAVLPTRCPH PGEACVVSGW GLVSHNEPGT AGSPRSQVSL PDTLHCANIS IISDTSCDKS YPGRLTNTMV CAGAEGRGAE SCEGDSGGPL VCGGILQGIV SWGDVPCDNT TKPGVYTKVC HYLEWIRETM KRNHHHHHH.

Product Science Overview

Genetic and Molecular Characteristics

KLK15 is located on chromosome 19, within a cluster of kallikrein genes. The gene encoding KLK15 contains multiple polyadenylation sites, and alternative splicing results in various transcript variants encoding different isoforms . The human recombinant form of KLK15 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain consisting of 249 amino acids (17-256 a.a.) with a molecular mass of approximately 27.4 kDa .

Expression and Purification

The recombinant KLK15 is expressed with a 6-amino acid His tag at the C-terminus, which facilitates its purification using chromatographic techniques . The protein is typically provided as a sterile, filtered, colorless solution in phosphate-buffered saline (PBS) with 10% glycerol, and it is recommended to store it at 4°C for short-term use or at -20°C for long-term storage .

Biological Significance

KLK15 is overexpressed in prostate cancer and is therefore considered a potential diagnostic or prognostic marker for this disease . The enzyme’s role in cancer biology is an area of active research, as understanding its function and regulation could lead to new therapeutic strategies.

Structural and Functional Properties

The amino acid sequence of KLK15 includes several key regions that contribute to its enzymatic activity. The protein’s structure allows it to interact with specific substrates, leading to the cleavage of peptide bonds. The recombinant form produced in Sf9 cells retains these functional properties, making it a valuable tool for laboratory research .

Applications in Research

KLK15 is used in various research applications, including studies on its role in cancer progression, its potential as a biomarker, and its enzymatic properties. The recombinant form allows researchers to investigate these aspects in a controlled environment, providing insights into the enzyme’s function and potential therapeutic uses .

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