Detects human SUMF1 in direct ELISAs and Western blots. In these formats, approximately 45% cross-reactivity with recombinant mouse SUMF1 is observed and less than 1% cross-reactivity with recombinant human SUMF2 is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human SUMF1 isoform 1 Ser34-Asp374 with a Ser63Asn substitution Accession # Q8NBK3
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Detection of Human Sulfatase Modifying Factor 1/SUMF1 by Western Blot.
Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line, Jurkat human acute T cell leukemia cell line, K562 human chronic myelogenous leukemia cell line, MCF‑7 human breast cancer cell line, and Raji human Burkitt's lymphoma cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Sulfatase Modifying Factor 1/SUMF1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3680) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). Specific bands were detected for Sulfatase Modifying Factor 1/SUMF1 at approximately 40 and 55 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Sulfatase Modifying Factor 1/SUMF1
Human SUMF-1 (also FGE) is a 42 kDa (341 aa), Ca++-binding
member of the sulfatase-modifying factor family. It is a soluble ER
lumenal glycoprotein that converts inactive sulfatases into an active
form by transforming a catalytic site cysteine into a formylglycine
residue. In the ER, SUMF-1 can exist as either a monomer, or a
disulfide-linked homodimer or a heterodimer with SUMF-2. Three splice
isoforms are known. Mature human SUMF-1 shares 90% aa sequence identity
with mouse SUMF-1.
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