ASRGL1 Human

ASRGL1 Human Recombinant
Cat. No.
BT27601
Source
Escherichia Coli.
Synonyms

ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

Appearance
Sterile Filtered colorless 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

ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.
ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

The ASRGL1 protein, comprising 308 amino acids, belongs to the Ntn-hydrolase family. Identified as an autoantigenic protein, ASRGL1 is found in the sperm's mid-piece following obstruction of the male reproductive tract. While primarily abundant in the testis, ASRGL1 expression is also observed in the brain, kidney, and gastrointestinal tissues. Notably, elevated levels of ASRGL1 are detected in ovarian, uterine, and mammary tumors compared to their corresponding normal tissues.

Description
Recombinant human ASRGL1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 331 amino acids (1-308 a.a). With a molecular mass of 34.4 kDa, ASRGL1 is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for sterility.
Formulation
The ASRGL1 protein solution is provided at a concentration of 0.5 mg/ml. The solution is buffered with phosphate-buffered saline (pH 7.4) and contains 10% glycerol and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For extended storage, freezing at -20°C is recommended. To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is advisable. Repeated freezing and thawing should be avoided.
Purity
The purity of the ASRGL1 protein is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms

ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.

Product Science Overview

Structure and Expression

The recombinant human ASRGL1 protein is typically expressed in Escherichia coli and is available in a full-length form, ranging from amino acids 1 to 308 . It is purified to a high degree, with a purity level exceeding 90%, making it suitable for various applications such as SDS-PAGE and mass spectrometry (MS) .

Enzymatic Activities

ASRGL1 exhibits both L-asparaginase and beta-aspartyl peptidase activities . The L-asparaginase activity involves the hydrolysis of L-asparagine to L-aspartate and ammonia, which is crucial for the metabolism of asparagine. The beta-aspartyl peptidase activity, on the other hand, involves the cleavage of beta-aspartyl dipeptides and their methyl esters . This dual enzymatic activity is essential for the production of L-aspartate, which can act as an excitatory neurotransmitter in certain brain regions .

Biological Significance

ASRGL1 is involved in several biological processes, including the production of L-aspartate, which is important for neurotransmission . It is highly active with substrates such as L-Asp beta-methyl ester and has catalytic activity towards various beta-aspartyl dipeptides . However, it does not exhibit activity towards aspartylglucosaminidase or glutamine .

Clinical and Research Applications

The recombinant form of ASRGL1 is widely used in research to study its enzymatic properties and potential therapeutic applications. Its high purity and specific activity make it a valuable tool for biochemical assays and structural studies .

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