Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
HMBS encodes a member of the hydroxymethylbilane synthase superfamily. Additionally we are shipping Hydroxymethylbilane Synthase Proteins (12) and Hydroxymethylbilane Synthase Kits (7) and many more products for this protein.
Showing 10 out of 76 products:
Cow (Bovine) Polyclonal HMBS Primary Antibody for WB - ABIN2785719
Kuo, Lee, Chuang, Huang: Acute intermittent porphyria with peripheral neuropathy: a follow-up study after hematin treatment. in Journal of the neurological sciences 2007
Show all 2 references for ABIN2785719
Cow (Bovine) Polyclonal HMBS Primary Antibody for WB - ABIN2785718
Malone, Rosman, Szoke, Davis: Myelination of brain in experimental hypothyroidism. An electron-microscopic and biochemical study of purified myelin isolates. in Journal of the neurological sciences 1975
Show all 2 references for ABIN2785718
Human Polyclonal HMBS Primary Antibody for IF, WB - ABIN516532
Anand, Wilson, Hasan, Maytin: Vitamin D3 enhances the apoptotic response of epithelial tumors to aminolevulinate-based photodynamic therapy. in Cancer research 2011
The interactions observed between the two pyrrole rings of the HEMC dipyrromethane cofactor and the active-site residues are highly specific and are most likely to represent the catalytically relevant binding mode.
Porphobilinogen deaminase deficiency alters vegetative and reproductive development and causes lesions in Arabidopsis.
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana. [porphobilinogen deaminase]
ALAS1 (show ALAS2 Antibodies) mRNA and activity were elevated approximately ~3- and 5-fold, and HMB synthase activity was approximately half-normal (~42%)
in the hepatic cancer tissue of two acute porphyria patients, somatic second-hit mutations result in nearly complete inactivation of PPOX (show OX Antibodies) and HMBS
study of hydroxymethylbilane synthase mutations and polymorphisms in Brazilian families with acute intermittent porphyria
Letter/Case Report: R173W mutation of HMBS gene can cause rhabdomyolysis in patients with variant acute intermittent porphyria.
we report a novel PBGD missense mutation.
Novel porphobilinogen deaminase gene mutations have been described in Polish patients with non-erythroid acute intermittent porphyria.
Conformational stability and activity of hydroxymethylbilane synthase (HMSB) and the acute intermittent porphyria K132N and V215E HMSB mutations.
Dense geographic aggregation with one identical haplotype strongly suggests a remote founder phenomenon for these Venezuelan acute intermittent porphyria families, carrying an unreported but most frequent HMBS mutation.
Findings indicate that using TATA-binding protein (TBP (show TBP Antibodies)) alone or in combination with hydroxymethylbilane synthase (HMBS) as endogenous controls could be a reliable method for normalizing qRT-PCR data in hepatoma cell lines treated with TNF-alpha (show TNF Antibodies).
The novel mutations of HMBS gene were three missense (R26L, R173G and D178H), two frameshift (c.749_765dup and c.874insC) and one intronic deletion (IVS12+3_+11delAGGGCCTGT).
PBGD-deficient mice showed a different response to fasting as measured by altered carbohydrate metabolism in the liver and modified glucose consumption in the brain cortex. Glucose homeostasis in fasted PBGD-deficient mice was efficiently normalized after restoration of PBGD gene expression in the liver.
Porphobilinogen deaminase over-expression in hepatocytes, albeit in a low proportion, reduced precursor accumulation, which is the hallmark of acute porphyric attacks.
PBGD-deficient mice were characterized biochemically during phenobarbital induction of heme synthesis and enzyme replacement.
This gene encodes a member of the hydroxymethylbilane synthase superfamily. The encoded protein is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. Mutations in this gene are associated with the autosomal dominant disease acute intermittent porphyria. Alternatively spliced transcript variants encoding different isoforms have been described.
, hydroxymethylbilane synthase
, Hydroxymethylbilane synthase
, porphobilinogen deaminase-like
, Porphobilinogen deaminase
, porphyria, acute; Chester type
, pre-uroporphyrinogen synthase
, uroporphyrinogen I synthase
, uroporphyrinogen I synthetase
, alternative name: porphobilinogen deaminase