SUMF1 Human, Sf9

Sulfatase Modifying Factor 1 Human Recombinant, Sf9
Cat. No.
BT23260
Source

Sf9, Insect cells.

Synonyms

SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 85.0% 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

SUMF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing  347 amino acids (34-374.a.) and having a molecular mass of  38.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). SUMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
SUMF1, a member of the SUMF protein family, plays a crucial role in the activation of sulfatases. It catalyzes the conversion of a cysteine residue in the active site of substrate sulfatases to 3-oxoalanine (C-alpha-formylglycine), which is essential for their enzymatic activity. Mutations in the SUMF1 gene can lead to multiple sulfatase deficiency, a lysosomal storage disorder characterized by the deficiency of multiple sulfatase enzymes.
Description
SUMF1, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 38.1 kDa. The recombinant protein encompasses amino acids 34 to 374 and includes a 6-amino acid His tag at the C-terminus. Its apparent molecular size on SDS-PAGE is approximately 40-57 kDa. SUMF1 is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
SUMF1 protein is supplied as a 0.25 mg/ml solution in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of SUMF1 is greater than 85.0% as determined by SDS-PAGE.
Synonyms

SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.

Source

Sf9, Insect cells.

Amino Acid Sequence

SQEAGTGAGA GSLAGSCGCG TPQRPGAHGS SAAAHRYSRE ANAPGPVPGE RQLAHSKMVP IPAGVFTMGT DDPQIKQDGE APARRVTIDA FYMDAYEVSN TEFEKFVNST GYLTEAEKFG DSFVFEGMLS EQVKTNIQQA VAAAPWWLPV KGANWRHPEG PDSTILHRPD HPVLHVSWND AVAYCTWAGK RLPTEAEWEY SCRGGLHNRL FPWGNKLQPK GQHYANIWQG EFPVTNTGED GFQGTAPVDA FPPNGYGLYN IVGNAWEWTS DWWTVHHSVE ETLNPKGPPS GKDRVKKGGS YMCHRSYCYR YRCAARSQNT PDSSASNLGF RCAADRLPTM DHHHHHH.

Product Science Overview

Gene and Protein Structure

The SUMF1 gene is located on chromosome 3p26.1 in humans . The gene encodes a protein that is part of the SUMF protein family. The primary function of SUMF1 is to catalyze the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, also known as C-alpha-formylglycine .

Function and Mechanism

SUMF1 is essential for the activation of sulfatases, which are enzymes that catalyze the hydrolysis of sulfate esters such as glycosaminoglycans, sulfolipids, and steroid sulfates . The catalytic residue in the active site of eukaryotic sulfatases, C-alpha-formylglycine (FGly), is post-translationally generated from a cysteine by SUMF1 in the endoplasmic reticulum (ER) . This modification is critical for the proper functioning of sulfatases.

Clinical Significance

Mutations in the SUMF1 gene can lead to multiple sulfatase deficiency (MSD), a lysosomal storage disorder . This condition results from the inability to form the FGly residue, leading to inactive sulfatases and the accumulation of sulfated substrates in lysosomes . MSD is characterized by a range of symptoms, including developmental delays, skeletal abnormalities, and neurological deficits .

Recombinant SUMF1 (Sf9)

Recombinant SUMF1 produced in Sf9 cells (a cell line derived from the fall armyworm, Spodoptera frugiperda) is used for research and therapeutic purposes . The recombinant form retains the enzymatic activity necessary for the post-translational modification of sulfatases, making it a valuable tool for studying the function and regulation of these enzymes .

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